نتایج جستجو برای: Yeast iso-1-cytochrome-c

تعداد نتایج: 3530424  

Journal: :Journal of Biological Chemistry 1980

Journal: :The Journal of biological chemistry 1985
C Visco H Taniuchi B S Berlett

Two forms of yeast cytochrome c synthetases with different specificities were resolved, one (synthetase I), solubilized from mitochondria or the cell debris with Triton X-100, recognizing not horse apocytochrome c but yeast apo-iso-1-cytochrome c as a substrate and the other (synthetase II) still bound with the particulate fraction from mitochondria after treatment with Triton, recognizing both...

Journal: :Journal of Biological Chemistry 1981

Journal: :Proceedings of the National Academy of Sciences of the United States of America 1980
D L Montgomery D W Leung M Smith P Shalit G Faye B D Hall

The two apocytochrome c proteins of yeast are coded for by separate genes. Iso-2-cytochrome c differs from the iso-1 protein at 17 positions within a homologous sequence of 108 amino acids. The previously cloned iso-1-cytochrome c coding sequence has been used to identify lambda-yeast recombinant phage containing the gene for iso-2-cytochrome c. The latter protein contains the dipeptide Ala-Ala...

Cytochrome-c (cyt-c) is an electron transport protein, and it is present throughout the evolution. More than 280 sequences have been reported in the protein sequence database (www.uniprot.org). Though sequentially diverse, cyt-c has essentially retained its tertiary structure or fold. Thus a vast data set of varied sequences with retention of similar structure and fun...

Journal: :biomacromolecular journal 2015
faizan ahmad sobia zaidi md imtaiyaz hassan asimul islam

cytochrome-c (cyt-c) is an electron transport protein, and it is present throughout the evolution. more than 280 sequences have been reported in the protein sequence database (www.uniprot.org). though sequentially diverse, cyt-c has essentially retained its tertiary structure or fold. thus a vast data set of varied sequences with retention of similar structure and function makes it a primary ca...

Journal: :The Biochemical journal 1994
T I Koshy T L Luntz B Plotkin A Schejter E Margoliash

The residue asparagine-52 of rat cytochrome c and baker's yeast iso-1-cytochrome c was mutated to isoleucine by site-directed mutagenesis, and the unfolding of the wild-type and mutant proteins in urea or guanidinium chloride solutions was studied. Whereas the yeast mutant cytochrome unfolded in 4-7 M urea with a rate constant (k) of 1.7 x 10(-2) s-1, the rat mutant protein unfolded with k = 5....

2003
C. HELMS

The CYC7-1 mutation in the yeast Saccharomyces cereuisiae causes the production of approximately 30 times the normal amount of iso-2-cytochrome c. Genetic analysis established that the CYC7-I mutation is a reciprocal translocation involving the left arm of chromosome V and the right arm of chromosome XVZ. The chromosome V arm was broken adjacent to the gene CYC7, which determines the primary st...

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