PRODUCTION AND PURIFICATION OF A GRANULAR-STARCH-BINDING DOMAIN OF GLUCOAMYLASE-1 FROM ASPERGILLUS-NIGER

被引：56

作者：

BELSHAW, NJ ^{[1
]}

WILLIAMSON, G ^{[1
]}

机构：

[1] INST FOOD RES, NORWICH NR4 7UA, NORFOLK, ENGLAND

来源：

FEBS LETTERS | 1990年 / 269卷 / 02期

关键词：

Aspergillus niger; Binding domain; Glucoamylase; Proteolysis; Starch binding;

D O I：

10.1016/0014-5793(90)81191-P

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：

A domain of glucoamylase 1 from Aspergillus niger which binds to granular starch was produced by proteolytic digestion and purified to apparent homogeneity by extraction with corn starch followed by anion-exchange chromatography and gel filtration. The peptide has a molecular weight of 25100, contains approximately 38% carbohydrate ( w w) and corresponds to residues 471-616 at the C-terminus of glucoamylase 1. The peptide bound to granular corn starch maximally at 1.08 nmol mg starch. It inhibited the hydrolysis of granular starch by glucoamylase 1 but had no effect on the hydrolysis of starch in solution. © 1990.

引用

页码：350 / 353

页数：4

共 20 条

[1] MICRO-SEQUENCE ANALYSIS OF PEPTIDES AND PROTEINS USING 4-NN-DIMETHYLAMINOAZOBENZENE 4'-ISOTHIOCYANATE-PHENYLISOTHIOCYANATE DOUBLE COUPLING METHOD [J].