PURIFICATION AND CHARACTERIZATION OF AN ABUNDANT RUBBER PARTICLE PROTEIN FROM GUAYULE

被引：28

作者：

BACKHAUS, RA ^{[1
]}

CORNISH, K ^{[1
]}

CHEN, SF ^{[1
]}

HUANG, DS ^{[1
]}

BESS, VH ^{[1
]}

机构：

[1] USDA ARS,WESTERN REG RES CTR,BERKELEY,CA 94710

来源：

PHYTOCHEMISTRY | 1991年 / 30卷 / 08期

关键词：

PARTHENIUM-ARGENTATUM; ASTERACEAE; GLYCOPROTEIN; ISOPENTENYL PYROPHOSPHATE; RUBBER PARTICLES; RUBBER TRANSFERASE;

D O I：

10.1016/0031-9422(91)85088-H

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：

Guayule rubber particles, which have high rubber transferase (RuT) activity, contain several characteristic proteins. The most abundant of these was purified by preparative gel electrophoresis and characterized. Designated the rubber particle protein (RPP), it is present in all guayule lines studied to date. RPP has an apparent M(r) of 48 500 and an isoelectric point of pI 6.2 which corresponds to a pI of 6.17 predicted by amino acid analysis. Antibodies were raised successfully against RPP and used for immunological analysis. Concanavalin A binds to blotted RPP indicating that it is a glycoprotein. When concanavalin A is added to purified rubber particles, it results in their rapid agglutination. However, protease treatments of purified rubber particles indicate that RPP is positioned inside the particle. Thus, it appears that RPP is positioned within the rubber particle, but at the surface, and that its oligosaccharide moiety extends to the particle exterior.

引用

页码：2493 / 2497

页数：5

共 23 条

[1] NEW ASPECTS OF RUBBER BIOSYNTHESIS [J].