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
收藏
页码：75 / 80
页数：6
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