摘要
用CM Cellulose 2 3柱层析分离纯化了 6 15小鼠珠蛋白α链 ,测定其N端氨基酸残基为缬氨酸 .6 15小鼠珠蛋白α链含有 141个氨基酸残基 ,其中 19个亮氨酸残基 ,10个组氨酸残基 ,9个缬氨酸残基 ,上述氨基酸残基的数目与文献中其亲本C57BL不同 .用胰蛋白酶水解 6 15小鼠珠蛋白α链 ,发现有不溶性的‘核心’和可溶性的酶解片段 .其中一个酶解肽段从N端数第 8位氨基酸残基发生了突变 ,由亲本的缬氨酸变为亮氨酸 .
The α chain of hemoglobin of 615 mouse was isolated and purified on CM Celullose 23 colomn chromatography. The N terminal amino acid of the α chain was valine determined with DABITC/PITC method.The amino acid composition was determined and it was different from the parent(C 57 BL)in literature on the number of leucine residue,histine residue and valine residue.An undissoluble ‘core’ and dissoluble peptides were found when the α chain of 615 mouse was hydrolysised by trypsin and it was found that the eighth amino acid residue from N terminal of one particular peptide fragment mutated from valine (C 57 BL) to leucine.
出处
《生物化学与生物物理进展》
SCIE
CAS
CSCD
北大核心
2001年第2期259-262,共4页
Progress In Biochemistry and Biophysics
