从感染根瘤菌的猪屎豆根瘤中纯化豆血红蛋白。

Purification of leghemoglobin from nodules of Crotalaria infected with Rhizobium.

作者信息

Mendonça E H, Mazzafera P, Schiavinato M A

机构信息

Departamento de Fisiologia Vegetal, Universidade Estadual de Campinas, SP, Brazil.

出版信息

Phytochemistry. 1999 Jan;50(2):313-6. doi: 10.1016/s0031-9422(98)00532-9.

DOI:10.1016/s0031-9422(98)00532-9

PMID:9933947

Abstract

The leghemoglobin from nodules of Crotalaria juncea infected with Rhizobium spp. was purified to homogeneity. The protein was purified after precipitation with 40-80% (NH4)2SO4, and chromatography by anionic exchange and gel filtration. The leghemoglobin has a single component and showed an apparent M(r) of ca. 17,300 and 23,700 determined by SDS-PAGE and gel filtration, respectively. The amino acid composition showed that asparagine/aspartic acid, glutamine/glutamic acid, alanine, lysine, serine and leucine were the main amino acids. Iron was detected only in the band corresponding to the purified protein. The N-terminal amino acid sequence for the first 19 residues showed high similarities with several other leghemoglobins from other plants.

摘要

从感染根瘤菌的菽麻根瘤中纯化出的豆血红蛋白达到了均一性。该蛋白质经40 - 80%硫酸铵沉淀、阴离子交换色谱和凝胶过滤后得以纯化。豆血红蛋白为单一成分，通过SDS - PAGE和凝胶过滤分别测定其表观分子量约为17,300和23,700。氨基酸组成表明，天冬酰胺/天冬氨酸、谷氨酰胺/谷氨酸、丙氨酸、赖氨酸、丝氨酸和亮氨酸是主要氨基酸。仅在与纯化蛋白对应的条带中检测到铁。前19个残基的N端氨基酸序列与其他植物的几种豆血红蛋白具有高度相似性。