FREE AND PROTEIN-BOUND BETA-AMYLASES OF BARLEY-GRAIN - CHARACTERIZATION BY 2-DIMENSIONAL IMMUNOELECTROPHORESIS

被引：45

作者：

HEJGAARD, J ^{[1
]}

机构：

[1] TECH UNIV DENMARK, DEPT BIOCHEM & NUTR, DK-2800 LYNGBY, DENMARK

来源：

PHYSIOLOGIA PLANTARUM | 1976年 / 38卷 / 04期

关键词：

D O I：

10.1111/j.1399-3054.1976.tb04006.x

中图分类号：

Q94 [植物学];

学科分类号：

071001 ;

摘要：

The .beta.-amylases of ungerminated barley (Hordeum distichum L. cv. ''Emir'') were characterized by 2-dimensional immunoelectrophoretic techniques in order to elucidate the structure and physiological importance of the latent .beta.-amylase present in cereal grains. Two water-soluble forms with partial immunochemical identity were detected. One of the enzyme forms was found to consist of aggregates between .beta.-amylase and an immunochemically distinct non-active protein. .beta.-Amylase and the protein could be released from the aggregates with .beta.-mercaptoethanol and, to some extent, with papain. .beta.-Mercaptoethanol increased the extractability of .beta.-amylase and of the non-active protein. The aggregated form of .beta.-amylase predominated in extracts made in the presence of papain. Possible functions of the non-enzymatic protein in formation of latent .beta.-amylase are discussed.

引用

页码：293 / 299

页数：7

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