Isolation, partial purification, and characterization of a novel petromyzonol sulfotransferase from Petromyzon marinus (lamprey) larval liver

We have isolated, partially purified, and characterized the 5α–petromyzonol (5α-PZ), (5α-cholan- 3α, 7α, 12α, 24-tetrahydroxy-) sulfotransferase (PZ-SULT) from larval lamprey liver. Crude liver extracts exhibited a PZ-SULT activity of 0.9120 pmol/min/mg in juvenile and 12.62 pmol/min/mg in larvae. Using crude larval liver extracts and various 5 β-cholan substrates and allocholic acid there was negligible activity, however, with 5α-PZ and 3-keto-5α-PZ the SULT activity was 231.5 pmol/min/mg and 180.8 pmol/min/mg respectively. This established that the sulfotransferase of lamprey larval liver extracts prefers (5 α) substrates and it is selective for hydroxyl at C-24. PZ-SULT was purified through various chromatography procedures. Partially purified PZ-SULT exhibited a pH optimum of 8.0, a temperature optimum of 22°C, and activity was linear for 1h. PZ-SULT exhibited a Km of 2.5 μM for PAPS and a Km of 8 μM for PZ. The affinity purified peak PZ-SULT exhibited a specific activity of 2,038 pmol/min/mg. The peak protein upon SDS-PAGE, correlated to an Mw 47 kDa. Photoaffinity labeling with PAP35S, specifically crosslinked the 47 kDa protein, further confirming the identity of PZ-SULT.Partial amino acid sequencing of the putative 47 kDa PZ-SULT protein yielded a peptide sequence (M)SISQAVDAAFXEI, which possessed an overall (∼35–40%) homology with mammalian SULT2B1a. We have isolated, partially purified, and characterized the 5α–petromyzonol (5α-PZ), (5α-cholan- 3α, 7α, 12α, 24-tetrahydroxy-) sulfotransferase (PZ-SULT) from larval lamprey liver. Crude liver extracts exhibited a PZ-SULT activity of 0.9120 pmol/min/mg in juvenile and 12.62 pmol/min/mg in larvae. Using crude larval liver extracts and various 5 β-cholan substrates and allocholic acid there was negligible activity, however, with 5α-PZ and 3-keto-5α-PZ the SULT activity was 231.5 pmol/min/mg and 180.8 pmol/min/mg respectively. This established that the sulfotransferase of lamprey larval liver extracts prefers (5 α) substrates and it is selective for hydroxyl at C-24. PZ-SULT was purified through various chromatography procedures. Partially purified PZ-SULT exhibited a pH optimum of 8.0, a temperature optimum of 22°C, and activity was linear for 1h. PZ-SULT exhibited a Km of 2.5 μM for PAPS and a Km of 8 μM for PZ. The affinity purified peak PZ-SULT exhibited a specific activity of 2,038 pmol/min/mg. The peak protein upon SDS-PAGE, correlated to an Mw 47 kDa. Photoaffinity labeling with PAP35S, specifically crosslinked the 47 kDa protein, further confirming the identity of PZ-SULT. Partial amino acid sequencing of the putative 47 kDa PZ-SULT protein yielded a peptide sequence (M)SISQAVDAAFXEI, which possessed an overall (∼35–40%) homology with mammalian SULT2B1a. In mammals, bile acids and salts are synthesized in the liver and stored in the gall bladder (1Borgstrom B. Barrowman J.A. Lindstrom M. Roles of bile acids in intestinal lipid digestion and absorption.in: Sterols and Bile Acids. Elsevier, Amsterdam1985: 405-425Crossref Scopus (39) Google Scholar) and aid in solubilizing fats, which facilitates lipolysis (2Borgström B. Influence of bile salt, pH and time on the action of pancreatic lipase: physiological implications.J. Lipid Res. 1992; 5: 522-531Abstract Full Text PDF Google Scholar). A substituent in cyclopentanoperhydrophenanthrene nucleus (3Hofmann A.F. Sjovall J. Kurz G. Radominska A. Schteingert C.D. Tint G.S. Vlahcevic Z.R. Setchell K.D. A proposed nomenclature for bile acids.J. Lipid Res. 1992; 33: 599-604Abstract Full Text PDF PubMed Google Scholar) that is above the plane is termed β, whereas a substituent that is below the plane is α oriented. The hydrogen attached to carbon-5 (C-5) can be either α or β oriented (4Carey M.C. Physical-chemical properties of bile acids and their salts.in: Sterols and Bile Acids. Elsevier, Amsterdam1985: 345-403Crossref Scopus (80) Google Scholar). The α hydrogen at C-5 results in trans fusion of the ring structure, yielding nearly a planar structure (5Haselwood G.A.D. Bile salt evolution.J. Lipid Res. 1967; 8: 535-550Abstract Full Text PDF PubMed Google Scholar, 6Hay D.W. Carey M.C. Chemical species of lipids in bile.Hepatology. 1990; 12: 6-12Google Scholar), e.g., allocholic acid (ACA)(7Haselwood G.A.D. Tokes L. Comparative studies of bile salts. Bile salts of the lamprey Petromyzon marinus L.Biochem. J. 1969; 114: 179-184Crossref PubMed Scopus (57) Google Scholar). Higher (C-27) bile acids and bile alcohols (also called cholestanes) are found in many organisms. For example, in the small skate Raja erinacea, the major sulfated bile alcohol is scymnol sulfate [3α,7α,12α, 24ξ,26,27-hexahydroxy-5β-cholestane-26 (27) sulfate] (8Karlaganis G. Bradley S.E. Boyer J.L. Batta A.K. Salen G. Egestad B. Sjovall J. A bile alcohol sulfate as a major component in the bile of the small skate (Raja erinacea).J. Lipid Res. 1989; 30: 317-322Abstract Full Text PDF PubMed Google Scholar). The partial purification and characterization of the enzyme that sulfonates 5β-scymnol from the liver of the shark Heterodontus portusjackson has been reported (9Macrides T.A. Faktor D.A. Kakafatis N. Amiet G. Enzymic sulfation of bile salts. Partial purification and characterization of an enzyme from the liver of the shark Heterodontus portusjacksoni that catalyzes the sulfation of the shark bile steroid 5β-scymnol.Comp. Biochem. Physiol. 1994; 1078: 461-469Google Scholar). In the coelacanth Latimera chalumnae, a 26-sulfate of latimerol (5α-cholestane-3β,7α,12α,26,27-pentol) and sulfate esters of 5α-cyprinol (5α-cholestane-3α,7α,12α,26,27-pentol) and 5α-bufol (5α-cholestane-3α,7α,12α,25,26-pentol) have been reported (10Kihira K. Akashi Y. Kuroki S. Yanagisawa J. Nakayama F. Hoshita T. Bile salts of the coelacanth, Latimera chalumnae.J. Lipid Res. 1984; 25: 1330-1336Abstract Full Text PDF PubMed Google Scholar). The identification of cyprinol sulfate from grass carp bile and its toxic effects in rats have been reported (11Hwang D-F. Yeh Y-H. Lai Y-H. Deng J-F. Identification of cyprinol and cyprinol sulfate from grass carp bile and their toxic effects in rats.Toxicon. 2001; 39: 411-414Crossref PubMed Scopus (18) Google Scholar). The West Indian manatee Trichechus manatus latirostris produces a sulfo-conjugate of 5α-cholestane-3α,6β,7α-25,26-pentol (12Kuroki S. Schteingart C.D. Hagey L.R. Cohen B.I. Mosbach E.H. Rossi S.S. Hofmann A.F. Matoba N. Une M. Hoshita T. Odell D.K. Bile salts of the West Indian manatee, Trichechus manatus latirostris: novel bile alcohol sulfates and absence of bile acids.J. Lipid Res. 1988; 29: 509-522Abstract Full Text PDF PubMed Google Scholar). The presence of various C-27 bile alcohols/salts in fish, amphibians, and mammals has been reported (13Hoshita T. Comparative biochemical studies of cholanoids.Yakugaku Zasshi. 1996; 116: 71-90Crossref PubMed Scopus (3) Google Scholar, 14Une M. Hoshita T. Natural occurrence and chemical synthesis of bile alcohols, higher bile acids, and short side chain bile acids.Hiroshima J. Med. Sci. 1994; 43: 37-67PubMed Google Scholar). Cholanes are 24-carbon (C-24) compounds, are similar to cholestanes (C-27), and can also possess hydrogen with an α or β orientation at position number 5, with the usual hydroxyls at 3, 7, and 12 (either α or β) and a carboxyl (bile acid) or hydroxyl (bile alcohol) group at position 24. 5α-PZ is a 5α-cholan-3α,7α,12α,24-tetrol (7Haselwood G.A.D. Tokes L. Comparative studies of bile salts. Bile salts of the lamprey Petromyzon marinus L.Biochem. J. 1969; 114: 179-184Crossref PubMed Scopus (57) Google Scholar). Petromyzonol (PZ) has been shown to be produced in copious amounts in Petromyzon marinus (lamprey), a jawless, boneless, primitive fish that belongs to the class of Agnatha. The 24-sulfonated derivative of PZ commonly called petromyzonol sulfate, (PZS) (15Li W. Sorensen P.W. Gallaher D.D. The olfactory system of migratory adult sea lamprey (Petromyzon marinus) is specifically and acutely sensitive to unique bile acids released by conspecific larvae.J. Gen. Physiol. 1995; 105: 569-587Crossref PubMed Scopus (163) Google Scholar, 16Polkinghorne C. Olson J.M. Gallaher D.G. Sorensen P.W. Larval sea lamprey release two unique bile acids to the water at a rate sufficient to produce detectable riverine pheromone plumes.Fish Physiol. Biochem. 2001; 24: 15-30Crossref Scopus (73) Google Scholar) and its derivative 5α-cholane-(7α,12α, dihydroxy)-3-one, 24-sulfate (3-keto-petromyzonol-sulfate, 3-keto-PZS, a more potent chemoattractant) have been shown to play a crucial roles as pheromones during the reproductive cycle of lampreys (17Li W. Scott A.P. Siefkes M.J. Yan H. Liu Q. Yun S-S. Gage D.A. Bile acid secreted by male sea lamprey that acts as a sex pheromone.Science. 2002; 296: 138-141Crossref PubMed Scopus (309) Google Scholar). The adult lamprey has been shown to rerurn to the same breeding ground for spawning by smelling the sulfonated derivatives of PZ produced by the larval lamprey. The sulfonate group at the C-24 is very crucial for its bioactivity as a chemoattractant (15Li W. Sorensen P.W. Gallaher D.D. The olfactory system of migratory adult sea lamprey (Petromyzon marinus) is specifically and acutely sensitive to unique bile acids released by conspecific larvae.J. Gen. Physiol. 1995; 105: 569-587Crossref PubMed Scopus (163) Google Scholar, 16Polkinghorne C. Olson J.M. Gallaher D.G. Sorensen P.W. Larval sea lamprey release two unique bile acids to the water at a rate sufficient to produce detectable riverine pheromone plumes.Fish Physiol. Biochem. 2001; 24: 15-30Crossref Scopus (73) Google Scholar, 17Li W. Scott A.P. Siefkes M.J. Yan H. Liu Q. Yun S-S. Gage D.A. Bile acid secreted by male sea lamprey that acts as a sex pheromone.Science. 2002; 296: 138-141Crossref PubMed Scopus (309) Google Scholar). The Great Lakes of North America are overpopulated with the vicious lamprey, which, as an adult, feeds on economically important teleosts (salmon, trout, etc.) by sucking the blood from these organisms. Thus, the predator lamprey is a menace to the fishing industry. One of the mechanisms for controlling the overpopulation of this organism is to use 5α-PZS and its derivative as the bait to trap adults. Knowledge of the biosynthesis and regulation of the 5α-PZS is very crucial to understanding the reproductive physiology of the lamprey so that eventually strategies can be sought to control the lamprey population. This paper is the first to report the isolation, partial purification, and characterization of a novel cholan-specific sulfotransferase (SULT) that is stereo selective (5α-cholan) and a regio-selective, C-24 hydroxyl-preferring enzyme from larval livers of lamprey. The radiochemical [35S]3′-phosphoadenosine 5′-phosphosulfate (PAPS) for enzyme assays was purchased from NEN Life Science Products or ARC, Inc. Cholan substrates ACA, 3-keto-PZ, PZS, nordesoxycholic acid (NDC), and 5α-PZ were purchased from Toronto Research Chemicals, Inc. (Toronto, Canada). 5α-PZ was also purchased from Cayman Co. (Ann Arbor, MI). 5β-24-ol, 5β-PZ was purchased from Steraloids, Inc. (Newport, RI). Cholic acid (CA), lithocholic acid (LCA), cholesterol, and deoxylithocholic acid (DLCA) were purchased from Sigma-Aldrich, Inc. DEAE ion exchange matrix (Macro-prep DEAE support) was purchased from Bio-Rad (Hercules, CA). Thin-layer chromatography PE silica gel G plates were obtained from Whatman (Clifton, NJ). Nu PAGE, 12% Bis-tris gels, and SDS-PAGE prestained protein molecular weight standards were obtained from Invitrogen (Carlsbad, CA). Larval and juvenile lamprey livers were shipped in by affinity molecular for gel and were also purchased from Sigma-Aldrich, Inc. The was in a of The of of enzyme and of PZ. The was at for 5 and by in water for 5 The were and were to silica gel chromatography plates and as the the chromatography plates were and to The were and the by were at larval livers were ground in of and from with a of a and The was with of and the were with the of the was in a a The was first at The was to at The was to and the was for PZ-SULT The extracts were a 5 ion exchange matrix DEAE support) and with A The was at a rate of with a of A of from to M. of was in were the by of was for PZ-SULT activity, as PZ-SULT activity of were and to a gel The was with and were at a rate of 12 PZ-SULT activity were further and an 5 to A of the was a affinity on The enzyme was through at and the the were to to the matrix for The was with A a salt 5 of to from the were by SDS-PAGE 12% Bis-tris were with to by Larval liver was purified through DEAE ion exchange in a similar to For affinity purification, the very peak was and the of the peak was This of many The very peak from the affinity enzyme and a were an 5 kDa A peak and a were for The was in a of The of in and 5 of activity of In a the an Photoaffinity labeling was from The were for at from CA). The was on and by of SDS-PAGE from The were by the at for 5 A was 12% Bis-tris were with to by For the were and to for The from SDS-PAGE were and with S. A 47 kDa was and amino by the a protein sequence was to The were small and with with of in acid for in the The were with acid for 12 and two with The the were The was for The acid PZ-SULT peptide was with SULT and protein sequence mammalian in the were and extracts from and were for PZ-SULT extracts from and the 5α-PZ exhibited negligible was higher PZ-SULT activity with 5α-PZ in with juvenile activity Using on PZ-SULT of larval liver various were for SULT The cholesterol, which is the of C-27 substrates and and substrates and the bile acid and 5β-24-ol, a bile sulfonated 5β-PZ possessed a negligible activity of pmol/min/mg. the a SULT activity of 231.5 pmol/min/mg. the activity was 180.8 pmol/min/mg. ACA, exhibited activity for is the same as the that at position it has a carboxyl group of a hydroxyl The PZ-SULT activity a temperature optimum of The activity was and linear for of at at pH and a pH optimum of The partially purified with ACA, and negligible activity, similar to that shown by crude extracts (SULT) activity in crude larval liver extracts various The were in The of the substrates in petromyzonol sulfate allocholic acid nordesoxycholic acid lithocholic acid and deoxylithocholic acid was in the the of temperature on PZ-SULT at temperature was for at pH to the in and of time on PZ-SULT at various time were at 22°C, pH The were by by at and the were to the in and of pH on the PZ-SULT were for at 22°C, of various that in the assays in and were for various and and and and and of temperature on PZ-SULT at temperature was for at pH to the in and of time on PZ-SULT at various time were at 22°C, pH The were by by at and the were to the in and of pH on the PZ-SULT were for at 22°C, of various that in the assays in and were for various and and and and and of temperature on PZ-SULT at temperature was for at pH to the in and of time on PZ-SULT at various time were at 22°C, pH The were by by at and the were to the in and of pH on the PZ-SULT were for at 22°C, of various that in the assays in and were for various and and and and and The and a PZ-SULT activity of pmol/min/mg was for protein chromatography a DEAE ion exchange the PZ-SULT peak activity at were and to further purification by gel PZ-SULT activity to The gel were an 5 of the PZ-SULT was to to a affinity and the were by with A The with a salt exhibited peak PZ-SULT activity The specific activity of the affinity PZ-SULT was found to be 2,038 pmol/min/mg. The peak PZ-SULT a 47 kDa protein and The that PZ-SULT activity the 47 kDa it the higher molecular weight gel chromatography purification of PZ-SULT. DEAE that PZ-SULT activity were and the gel The was with A at a rate of PZ-SULT activity in a from was is affinity chromatography purification of PZ-SULT. PZ-SULT from gel chromatography were and an and a was through the The through was to for The was and with 5 of A with to The activity that to the in a of The PZ-SULT activity in of affinity PZ-SULT. and which PZ-SULT activity, and which PZ-SULT activity, were by 12% Bis-tris SDS-PAGE and with molecular from by and to the major protein by the 3, which PZ-SULT activity, the 47 kDa For purification, the gel was it yielded in purification and in of from the DEAE ion exchange the activity from the peak were and further purified affinity This the of many the peak that the PZ-SULT activity was for as by SDS-PAGE and a 47 kDa PZ-SULT protein and a higher molecular weight were This PZ-SULT and a that PZ-SULT activity, with 47 kDa were for labeling with the and for the purified the a to 47 kDa. were and from the that PZ-SULT activity, were In labeling was the in the presence of PAPS was confirming the specific labeling by the PAPS of the Partially purified enzyme from DEAE ion exchange and affinity that of PZ-SULT activity were for the Km for PAPS and PZ. PZ and a of PAPS the PZ-SULT exhibited a Km of 8 μM for PZ at a of μM the PAPS was and the of was The PZ-SULT exhibited a Km of 2.5 μM for PAPS PZ-SULT 5′-phosphosulfate (PAPS) as DEAE chromatography by affinity enzyme was for PZ-SULT various of as in and the of two are shown in the PZ-SULT petromyzonol (PZ) as DEAE chromatography by affinity Partially purified enzyme was for PZ-SULT various of as in and the of two are shown in the PZ-SULT protein is Partial amino acid sequencing yielded a sequence of Partial amino acid of PZ-SULT with mammalian protein protein protein and protein an overall of to SULT2B1a. the sequence found in PZ-SULT is in two of the mammalian the for C-27 for SULT activity lamprey larval liver sulfonated similar to possess the usual at 3, 7, and and the at position is carboxyl (bile acid) or hydroxyl (bile alcohol) (4Carey M.C. Physical-chemical properties of bile acids and their salts.in: Sterols and Bile Acids. Elsevier, Amsterdam1985: 345-403Crossref Scopus (80) Google Scholar). primitive fish, as the lamprey and the fish, produce (13Hoshita T. Comparative biochemical studies of cholanoids.Yakugaku Zasshi. 1996; 116: 71-90Crossref PubMed Scopus (3) Google Scholar). The sulfo-conjugate (bile of PZ has been shown to as a chemoattractant for the spawning adult lamprey (15Li W. Sorensen P.W. Gallaher D.D. The olfactory system of migratory adult sea lamprey (Petromyzon marinus) is specifically and acutely sensitive to unique bile acids released by conspecific larvae.J. Gen. Physiol. 1995; 105: 569-587Crossref PubMed Scopus (163) Google Scholar). Thus, 5α-PZ can be to its structure and its to as a pheromone during the reproductive The and the of 5α-PZ and its as a chemoattractant (15Li W. Sorensen P.W. Gallaher D.D. The olfactory system of migratory adult sea lamprey (Petromyzon marinus) is specifically and acutely sensitive to unique bile acids released by conspecific larvae.J. Gen. Physiol. 1995; 105: 569-587Crossref PubMed Scopus (163) Google Scholar, 16Polkinghorne C. Olson J.M. Gallaher D.G. Sorensen P.W. Larval sea lamprey release two unique bile acids to the water at a rate sufficient to produce detectable riverine pheromone plumes.Fish Physiol. Biochem. 2001; 24: 15-30Crossref Scopus (73) Google Scholar, 17Li W. Scott A.P. Siefkes M.J. Yan H. Liu Q. Yun S-S. Gage D.A. Bile acid secreted by male sea lamprey that acts as a sex pheromone.Science. 2002; 296: 138-141Crossref PubMed Scopus (309) Google Scholar). larval and juvenile liver extracts were for PZ-SULT activity, the larval liver higher PZ-SULT this on the reproductive cycle of lampreys and the of as a lampreys to a very primitive group of fish as the a and a and their cycle a larval lamprey in the at the of and and for to can which an juvenile with a for a and a for and Thus, lamprey overpopulation is a major to the Great Lakes (15Li W. Sorensen P.W. Gallaher D.D. The olfactory system of migratory adult sea lamprey (Petromyzon marinus) is specifically and acutely sensitive to unique bile acids released by conspecific larvae.J. Gen. Physiol. 1995; 105: 569-587Crossref PubMed Scopus (163) Google Scholar, 16Polkinghorne C. Olson J.M. Gallaher D.G. Sorensen P.W. Larval sea lamprey release two unique bile acids to the water at a rate sufficient to produce detectable riverine pheromone plumes.Fish Physiol. Biochem. 2001; 24: 15-30Crossref Scopus (73) Google Scholar, 17Li W. Scott A.P. Siefkes M.J. Yan H. Liu Q. Yun S-S. Gage D.A. Bile acid secreted by male sea lamprey that acts as a sex pheromone.Science. 2002; 296: 138-141Crossref PubMed Scopus (309) Google Scholar). The of lampreys is of the The lampreys to in the that have spawning in the the of 5α-PZS lampreys are to produced by the male and use this as a for spawning C. Olson J.M. Gallaher D.G. Sorensen P.W. Larval sea lamprey release two unique bile acids to the water at a rate sufficient to produce detectable riverine pheromone plumes.Fish Physiol. Biochem. 2001; 24: 15-30Crossref Scopus (73) Google Scholar). The that the higher PZ-SULT activity be that the chemoattractant) to the as time in the breeding larval liver extracts were with various for of the substrates sulfonated for which above which is 5α-PZ This established that the larval liver extracts a enzyme with the substrates and 3-keto-5α-PZ sulfonated is the same as that the a group at the This that the at position the activity of SULT and that the is at the hydroxyl The sequence of the 5α-PZS and of the more potent chemoattractant 3-keto-5α-PZ have been The for the biosynthesis of C-27 5α-cyprinol has been and of the crucial have been T. acids and bile of to by carp Biochem. 1969; PubMed Scopus Google Scholar). the of the SULT activity of the two 5α-PZ and can that 5α-PZS is first and the the 5α-PZS the potent is the same as the that position is carboxyl of a hydroxyl sulfonated which established that the PZ-SULT prefers the hydroxyl group at the C-24 position for In which has hydroxyl at 3, 7, and 12 and has the to be sulfonated Thus, that the PZ-SULT in larval liver is a and also enzyme for The affinity PZ-SULT exhibited a specific activity of 2,038 pmol/min/mg and correlated with a of 47 kDa by This is the first report on the isolation, purification, and characterization of a novel SULT from The partially purified and characterized SULT from fish is a (C-27) 5β-scymnol from shark The 5β-scymnol SULT enzyme a molecular of kDa (9Macrides T.A. Faktor D.A. Kakafatis N. Amiet G. Enzymic sulfation of bile salts. Partial purification and characterization of an enzyme from the liver of the shark Heterodontus portusjacksoni that catalyzes the sulfation of the shark bile steroid 5β-scymnol.Comp. Biochem. Physiol. 1994; 1078: 461-469Google Scholar). The molecular is very to that of the petromyzonol lampreys are from mammalian in molecular from to kDa and molecular 2002; PubMed Scopus Google Scholar). the acid peptide sequence to putative PZ-SULT was with mammalian and and a protein the yielded a overall homology of is that the amino acid of the PZ-SULT is in mammalian SULT2B1a. The SULT is of which is in the of and The mammalian have that from to amino acids, whereas and of and amino acids, respectively. the and are at the amino acid Y. sulfate in it Lipid Res. Full Text Full Text PDF Scopus Google Scholar). Using a purified peak PZ-SULT activity labeling with was to the identity of PZ-SULT. Photoaffinity labeling the 47 kDa further confirming the of the PZ-SULT labeling of and has been A. J.M. S. Photoaffinity labeling of with 1996; Full Text Full Text PDF PubMed Scopus Google Scholar) exhibited a Km of 8 μM for PZ and 2.5 μM for in exhibited a Km of μM for PAPS and μM for 5β-scymnol (9Macrides T.A. Faktor D.A. Kakafatis N. Amiet G. Enzymic sulfation of bile salts. Partial purification and characterization of an enzyme from the liver of the shark Heterodontus portusjacksoni that catalyzes the sulfation of the shark bile steroid 5β-scymnol.Comp. Biochem. Physiol. 1994; 1078: 461-469Google Scholar). are very are from two is a (C-27) SULT and the is a (C-24) In this have a novel hydroxyl at the C-24 and have reported the characterization of the biochemical the overall biosynthesis of 5α-PZS is to understanding the reproductive cycle of lampreys and to at strategies for controlling the overpopulation of lampreys in the Great The for and and of of for their The the of for their in protein This was by a from the Great Lakes 5′-phosphosulfate petromyzonol petromyzonol sulfate petromyzonol sulfotransferase sulfotransferase

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