CAJ | 학술논문

用CM-Cellulose-23柱层析分离纯化了615小鼠珠蛋白α链，测定其N端氨基酸残基为缬氨酸.615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615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.
용CM-Cellulose-23주층석분리순화료615소서주단백α련，측정기N단안기산잔기위힐안산.615소서주단백α련함유141개안기산잔기，기중19개량안산잔기，10개조안산잔기，9개힐안산잔기,상술안기산잔기적수목여문헌중기친본C57BL불동.용이단백매수해615소서주단백α련，발현유불용성적‘핵심’화가용성적매해편단.기중일개매해태단종N단수제8위안기산잔기발생료돌변，유친본적힐안산변위량안산.
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(C57BL)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 (C57BL) to leucine.