Cleavage of γ-carboxyglutamyl peptide bonds by cyanogen bromide and byN-bromosuccinimide
نویسندگان
چکیده
منابع مشابه
Cyanogen Bromide Cleavage and Partial Amino Acid
When samples containing homoserine and homoserine lactone Porcine growth hormone has been cleaved with cyanogen were analyzed, the short column and the first part of the long bromide and the resulting fragments separated by gel filtracolumn (until glutamic acid emerged) were run at 50” instead of tion. The amino acid sequences of the amino-terminal the usua1 55”* Under these conditions homoseri...
متن کاملIsolation of cyanogen bromide cleavage peptides from myoglobins.
The chemical cleavage of apomyoglobins by the cyanogen bromide procedure1 has provided frag ments suitable for sequence analysis2; 3 and for studies of physical 4~6 and immunochemical pro perties 7. Offord 8 has used a peptide obtained from the cyanogen bromide cleavage of ribonuclease in studies aimed at the semi-synthesis of a protein. The purpose of this report is to present condi tions t...
متن کاملSite-selective chemical cleavage of peptide bonds.
Site-selective cleavage of extremely unreactive peptide bonds is a very important chemical modification that provides invaluable information regarding protein sequence, and it acts as a modulator of protein structure and function for therapeutic applications. For controlled and selective cleavage, a daunting task, chemical reagents must selectively recognize or bind to one or more amino acid re...
متن کاملCleavage of bacterial flagellin with cyanogen bromide. Chemical and physical properties of the protein fragments.
1. Flagellin, isolated from the flagella of Salmonella adelaide, was shown by various criteria to be a pure protein. It had a molecular weight of about 40000 and contained three methionine, six tyrosine, 11 arginine and 25 lysine residues/mol., of which 11 of the lysine residues were present as in-N-methyl-lysine. 2. After treatment of flagellin with cyanogen bromide in formic acid, four main f...
متن کاملBiological Activity of the Cleavage Product of Human Immunoglobulin G with Cyanogen Bromide
Treatment of human IgG with cyanogen bromide in 0.05 M HCl under specified conditions resulted in the cleavage of about half of its methionyl peptide bonds. A major fragment of about 5S was isolated from the reaction mixture by gel filtration in quantitative yield. The CNBr fragment reacted fully with goat antiserum against human light chain, but its reaction with anti-heavy chain was markedly ...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: FEBS Letters
سال: 1978
ISSN: 0014-5793
DOI: 10.1016/0014-5793(78)80073-8