PURIFICATION OF AN ANIONIC PEROXIDASE ISOENZYME FROM MANGO (MANGIFERA-INDICA L VAR CHAUNSA)

被引：16

作者：

KHAN, AA ^{[1
]}

ROBINSON, DS ^{[1
]}

机构：

[1] UNIV LEEDS,PROCTER DEPT FOOD SCI,LEEDS LS2 9JT,W YORKSHIRE,ENGLAND

来源：

FOOD CHEMISTRY | 1993年 / 46卷 / 01期

关键词：

D O I：

10.1016/0308-8146(93)90076-R

中图分类号：

O69 [应用化学];

学科分类号：

081704 ;

摘要：

A mango anionic peroxidase isoenzyme (A1) has been purified to homogeneity by salt fractionation, gel filtration and ion-exchange chromatography. The purified isolated enzyme was free from contaminating proteins and other isoperoxidases. The molecular weight of A1 was calculated to be approximately 40 000. The major amino acid residues were glycine, serine and glutamic acid, representing approximately 48% of the protein moiety.

引用

页码：61 / 64

页数：4

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