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Selective cleavage of N-terminal amino acid in a peptide by polymeric cobalt (III) triene complex.
Indian J Biochem Biophys ; 1989 Oct; 26(5): 348-9
Article in English | IMSEAR | ID: sea-28462
ABSTRACT
Cellulose was functionalized to incorporate triethylenetetramine group. This was in turn converted into the polymeric analogue of cobalt(III)triene complex. The polymeric complex reacts with peptides resulting in the cleavage of amino end amino acid, thus suggesting the applicability of the polymeric reagent as a solid phase reagent for N-terminal determination.
Subject(s)
Full text: Available Index: IMSEAR (South-East Asia) Main subject: Organometallic Compounds / Polymers / Proteins / Cobalt / Amino Acids / Hydrolysis Language: English Journal: Indian J Biochem Biophys Year: 1989 Type: Article

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Full text: Available Index: IMSEAR (South-East Asia) Main subject: Organometallic Compounds / Polymers / Proteins / Cobalt / Amino Acids / Hydrolysis Language: English Journal: Indian J Biochem Biophys Year: 1989 Type: Article