scholarly journals Rat liver glutathione S-transferases. Nucleotide sequence analysis of a Yb1 cDNA clone and prediction of the complete amino acid sequence of the Yb1 subunit.

1985 ◽  
Vol 260 (24) ◽  
pp. 13268-13271 ◽  
Author(s):  
G J Ding ◽  
A Y Lu ◽  
C B Pickett
Keyword(s):  
Amino Acid ◽  
Sequence Analysis ◽  
Nucleotide Sequence ◽  
Amino Acid Sequence ◽  
Rat Liver ◽  
Cdna Clone ◽  
Nucleotide Sequence Analysis ◽  
Liver Glutathione ◽  
Complete Amino Acid Sequence ◽  
Glutathione S Transferases

scholarly journals The complete amino acid sequence of yeast phosphoglycerate kinase

1983 ◽  
Vol 211 (1) ◽  
pp. 199-218 ◽  
Author(s):  
R E Perkins ◽  
S C Conroy ◽  
B Dunbar ◽  
L A Fothergill ◽  
M F Tuite ◽  
...  
Keyword(s):  
Amino Acid ◽  
Sequence Analysis ◽  
Amino Acid Sequence ◽  
Phosphoglycerate Kinase ◽  
Nucleotide Sequence Analysis ◽  
Crystallographic Structure ◽  
Phosphate Binding ◽  
Amino Acid Sequence Analysis ◽  
Complete Amino Acid Sequence ◽  
Tryptophan Residues

The complete amino acid sequence of yeast phosphoglycerate kinase, comprising 415 residues, was determined. The sequence of residues 1-173 was deduced mainly from nucleotide sequence analysis of a series of overlapping fragments derived from the relevant portion of a 2.95-kilobase endonuclease-HindIII-digest fragment containing the yeast phosphoglycerate kinase gene. The sequence of residues 174-415 was deduced mainly from amino acid sequence analysis of three CNBr-cleavage fragments, and from peptides derived from these fragments after digestion by a number of proteolytic enzymes. Cleavage at the two tryptophan residues with o-iodosobenzoic acid was also used to isolate fragments suitable for amino acid sequence analysis. Determination of the complete sequence now allows a detailed interpretation of the existing high-resolution X-ray-crystallographic structure. The sequence -Ile-Ile-Gly-Gly-Gly- occurs twice in distant parts of the linear sequence (residues 232-236 and 367-371). Both these regions contribute to the nucleoside phosphate-binding site. A comparison of the sequence of yeast phosphoglycerate kinase reported here with the sequences of phosphoglycerate kinase from horse muscle and human erythrocytes shows that the yeast enzyme is 64% identical with the mammalian enzymes. The yeast has strikingly fewer methionine, cysteine and tryptophan residues.

Cloning of metallothionein cDNA from neonatal rat liver

1982 ◽  
Vol 2 (10) ◽  
pp. 761-768 ◽  
Author(s):  
J. F. B. Mercer ◽  
P. Hudson
Keyword(s):  
Sequence Analysis ◽  
Nucleotide Sequence ◽  
Rat Liver ◽  
Cdna Clone ◽  
Untranslated Region ◽  
Neonatal Rat ◽  
Nucleotide Sequence Analysis ◽  
Coding Sequence ◽  
Rat Livers ◽  
I Gene

A metallothionein cDNA clone was isolated from a cDNA bank prepared from neonatal rat liver poly(A)-containing RNA by a colony screening procedure using [32P]cDNA probes prepared from mRNA of either metal-induced or uninduced rat livers. Nucleotide sequence analysis of this clone showed that it contained the entire 3′ untranslated region and 30% of the coding sequence for a rat metallothionein. The sequence is remarkably homologous with the mouse metallothionein-I gene.

Sign in / Sign up

Export Citation Format

Share Document