大师作文网求文献：Cho i K H,Laursen R A.Am ino-acid sequence and g ly can
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求文献：Cho i K H,Laursen R A.Am ino-acid sequence and g ly can structures o f cy ste ine proteases
Cho i K H,Laursen R A.Am ino-acid sequence and g ly can structures o f cy ste ine proteases with proline specificity from ginger rhizom e Zingiber officinale[ J].Eur J B iochem,2000,267( 5):1 516- 1 526
Cho i K H,Laursen R A.Am ino-acid sequence and g ly can structures o f cy ste ine proteases with proline specificity from ginger rhizom e Zingiber officinale[ J].Eur J B iochem,2000,267( 5):1 516- 1 526
你可以到NCBI中的pumed中搜索,这是我搜到的结果.不过需要付费才能得到全文.Amino-acid sequence and glycan structures of cysteine proteases with proline specificity from ginger rhizome Zingiber officinale.
Choi KH,Laursen RA.
SourceDepartment of Chemistry,Boston University,MA,USA.
Abstract
The ginger proteases (GP-I and GP-II),isolated from the ginger rhizome Zingiber officinale,have an unusual substrate specificity preference for cleaving peptides with a proline residue at the P2 position.The complete amino-acid sequence of GP-II,a glycoprotein containing 221 amino acids,and about 98% that of GP-I have been determined.Both proteases,which are 82% similar,have cysteine residues at positions 27 and histidines at position 161,corresponding to the essential cysteine-histidine diads found in the papain family of cysteine proteases,and six corresponding cysteine residues that form the three invariant disulfide linkages seen in this family of proteins.The sequence homology with other members (papain,bromelain,actinidin,protease omega,etc.) of this family is approximately 50%.GP-II has two predicted glycosylation sites at Asn99 and Asn156.Analyisis by electrospray and collision-induced dissociation MS showed that both sites were occupied by the glycans (Man)3(Xyl)1(Fuc)1(GlcNAc)2 and (Man)3(Xyl)1(Fuc)1(GlcNAc)3,in a ratio of approximately 7 :1.Both glycans are xylose containing biantennary complex types that share the common core structural unit,Man1-->6(Man1-->3) (Xyl1-->2)Man1-->4GlcNAc1-->4(Fuc1-->3)GlcNAc for the major form,with an additional N-acetylglucosamine residue being linked,in the minor form,to one of the terminal mannose units of the core structure.
PMID:10691991 [PubMed - indexed for MEDLINE] Free full text
Choi KH,Laursen RA.
SourceDepartment of Chemistry,Boston University,MA,USA.
Abstract
The ginger proteases (GP-I and GP-II),isolated from the ginger rhizome Zingiber officinale,have an unusual substrate specificity preference for cleaving peptides with a proline residue at the P2 position.The complete amino-acid sequence of GP-II,a glycoprotein containing 221 amino acids,and about 98% that of GP-I have been determined.Both proteases,which are 82% similar,have cysteine residues at positions 27 and histidines at position 161,corresponding to the essential cysteine-histidine diads found in the papain family of cysteine proteases,and six corresponding cysteine residues that form the three invariant disulfide linkages seen in this family of proteins.The sequence homology with other members (papain,bromelain,actinidin,protease omega,etc.) of this family is approximately 50%.GP-II has two predicted glycosylation sites at Asn99 and Asn156.Analyisis by electrospray and collision-induced dissociation MS showed that both sites were occupied by the glycans (Man)3(Xyl)1(Fuc)1(GlcNAc)2 and (Man)3(Xyl)1(Fuc)1(GlcNAc)3,in a ratio of approximately 7 :1.Both glycans are xylose containing biantennary complex types that share the common core structural unit,Man1-->6(Man1-->3) (Xyl1-->2)Man1-->4GlcNAc1-->4(Fuc1-->3)GlcNAc for the major form,with an additional N-acetylglucosamine residue being linked,in the minor form,to one of the terminal mannose units of the core structure.
PMID:10691991 [PubMed - indexed for MEDLINE] Free full text
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