Purification and some properties of alpha-galactosidase from Penicillum purpurogenum

被引：36

作者：

Shibuya, H

Kobayashi, H

Park, GG

Komatsu, Y

Sato, T

Kaneko, R

Nagasaki, H

Yoshida, S

Kasamo, K

Kusakabe, I

机构：

[1] UNIV TSUKUBA, INST APPL BIOCHEM, IBARAKI, OSAKA 305, JAPAN

[2] MINIST AGR FORESTRY & FISHERIES, NATL FOOD RES INST, IBARAKI, OSAKA 305, JAPAN

[3] KYUNGWON UNIV, DEPT FOOD SCI & TECHNOL, SONGNAN 461701, SOUTH KOREA

来源：

BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY | 1995年 / 59卷 / 12期

关键词：

D O I：

10.1271/bbb.59.2333

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：

alpha-Galactosidase was purified by ion-exchange chromatographies on DEAE-cellulose and SE-cellulose columns from the culture filtrate of Penicillium purpurogenum No. 618. The final preparation was judged homogeneous by SDS-PAGE and its molecular mass and isoelectric point were estimated to be 67 kDa and 4.1, respectively. The N-terminal amino acid sequence of the enzyme was analyzed and aligned with those of other alpha-galactosidases. In addition, the enzyme acted on the stubbed alpha-galactosyl residue connected to the beta-1,4-manno-oligosaccharide chain, indicating that this specificity was quite different from that of Mortierella vinacea alpha-galactosidase.

引用

页码：2333 / 2335

页数：3

共 9 条

[1] HUMAN ALPHA-GALACTOSIDASE-A - NUCLEOTIDE-SEQUENCE OF A CDNA CLONE ENCODING THE MATURE ENZYME [J].