Amino acid sequences of two sulfhydryl-containing tryptic peptides of the polypeptide chain elongation factor Tu

1975 ◽  
Vol 66 (3) ◽  
pp. 1069-1077 ◽  
Author(s):  
Shun Nakamura ◽  
Ken-ichi Arai ◽  
Kenji Takahashi ◽  
Yoshito Kaziro
1988 ◽  
pp. 259-269
Author(s):  
A. Parmeggiani ◽  
P. H. Anborgh ◽  
R. H. Cool ◽  
E. Jacquet ◽  
M. Jensen ◽  
...  

1978 ◽  
Vol 173 (1) ◽  
pp. 73-83 ◽  
Author(s):  
A Carne ◽  
C H Moore

The amino acid sequences of the tryptic peptides of the thiol proteinase actinidin from Actinidia chinensis were determined by the manual dansyl–Edman procedure. There are 12 tryptic peptides, which give a polypeptide chain of 220 residues with a mol.wt. of 23500. An alignment of the tryptic peptides was made by using the X-ray-crystallographic data of Baker [(1977) J. Mol. Biol. 115, 263–277] determined at 0.28 nm resolution on crystalline actinidin. Detailed evidence for the amino acid sequences of the tryptic peptides has been deposited as Supplementary Publication SUP 50083 (14 pages) at the British Library Lending Division, Boston Spa, Wetherby, West Yorkshire LS23 7BQ, U.K., from whom copies can be obtained on the terms indicated in Biochem. J. (1978) 169, 5.


1968 ◽  
Vol 46 (8) ◽  
pp. 825-843 ◽  
Author(s):  
David B. Smith

Evidence for the amino acid sequence of some peptides formed by the action of trypsin on the β-polypeptide chain of horse hemoglobin is presented. By analogy with the amino acid sequence of the β-chain of human hemoglobin, these peptides cover positions 1 to 82 and 117 to 146 of the horse β-chain. Twenty-one differences between the human and horse β-chain sequence are found in these regions.


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