SAPOSIN-C FROM BOVINE SPLEEN - COMPLETE AMINO-ACID-SEQUENCE AND RELATION BETWEEN THE STRUCTURE AND ITS BIOLOGICAL-ACTIVITY

被引：24

作者：

SANO, A ^{[1
]}

MIZUNO, T ^{[1
]}

KONDOH, K ^{[1
]}

HINENO, T ^{[1
]}

UENO, S ^{[1
]}

KAKIMOTO, Y ^{[1
]}

MORITA, N ^{[1
]}

机构：

[1] SHIMADZU CO LTD,DEPT BIOTECHNOL INSTRUMENTS,NAKAGYO,KYOTO,JAPAN

来源：

BIOCHIMICA ET BIOPHYSICA ACTA | 1992年 / 1120卷 / 01期

关键词：

AMINO ACID SEQUENCE; STRUCTURE-ACTIVITY RELATIONSHIP; SPLEEN; SAPOSIN-C; ACTIVATOR PROTEIN; GLYCOPROTEIN;

D O I：

10.1016/0167-4838(92)90426-E

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Saposin-C, a small acidic glycoprotein that can activate glucosylceramide-beta-glucosidase, has been isolated from bovine spleen. The complete amino acid sequence of bovine saposin-C was determined by Edman degradation of the purified protein and its fragmented peptides. It contains 80 amino acids, one carbohydrate chain attached to a single aspargine residue and six cysteine residues in oxidized form. The sequence of bovine saposin-C is 76 and 65% identical with the sequences of saposin-C from human spleen and guinea pig liver, respectively. Hydropathy profiles of the sequence of saposin-C from three species were similar despite the significant residue substitutions. Bovine saposin-C had a stronger effect in stimulating bovine beta-glucosidase compared to human saposin-C. However, the effect of human saposin-C in stimulating human enzyme was stronger than that of bovine saposin-C. The region around residue 35, which is next to the extremely hydrophilic region, seems to be important to produce an interaction with the enzyme.

引用

页码：75 / 80

页数：6

共 25 条

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