THE MAJOR ALBUMIN PROTEINS FROM PEA (PISUM-SATIVUM-L) - PURIFICATION AND SOME PROPERTIES
THE MAJOR ALBUMIN PROTEINS FROM PEA (PISUM-SATIVUM-L) - PURIFICATION AND SOME PROPERTIES
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DOI：
10.1042/bj2180795
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发表时间：
1984-01-01
影响因子：
4.1
通讯作者：
BOULTER, D
中科院分区：
文献类型：
--
作者：
CROY, RRD;HOQUE, MS;BOULTER, D
描述了一种分离豌豆白蛋白的方案。利用该方案，分离纯化了2个关系密切的主要白蛋白蛋白。较大的蛋白质命名为PMA-L，具有Mw.apprx。53,000兆瓦，由两个25,000兆瓦的亚基组成，而较小的PMA-S有兆瓦.apprx。48,000兆瓦，包含两个24,000兆瓦的亚基。通过免疫交叉反应、氨基酸组成、N-末端氨基酸、胰蛋白酶-多肽图谱和CNBr-裂解产物判断，没有证据表明这两个亚基大小的混合二聚体存在。两种蛋白质均含有大量的S氨基酸。这些蛋白质定位于子叶细胞的可溶性胞浆部分，对种子萌发没有明显的降解作用。初步筛选表明，在至少3个不同但密切相关的豆科植物中存在同源的主要白蛋白蛋白[野山豆、豆角豆属、雪松属植物]。
A scheme is described for the fractionation of pea albumin proteins. By using this scheme, 2 closely related major albumin proteins were isolated and purified to homogeneity. The larger protein, designated PMA-L, has MW .apprx. 53,000 and consists of two 25,000-MW subunits, whereas the smaller, PMA-S, has MW .apprx. 48,000 and contains two 24,000-MW subunits. There was no evidence of mixed dimers of the 2 subunit sizes, despite their close homology as judged by immunological cross-reaction, amino acid composition, N-terminal amino acids, tryptic-peptide mapping and CNBr-cleavage products. Both proteins contained significant amounts of S amino acids. The proteins were located in the soluble cytosol fraction of cotyledon cells and are not significantly degraded on seed germination. Preliminary screening indicates the presence of homologous major albumin proteins in at least 3 different, though closely related, legume species [Lathyrus odoratus, Lens culinaris, Cicer arietinum].