Literature DB >> 368598

A method for purification of peptides from hydrolysates of proteins modified by chemically active analogues of substrates containing cis-diol groups.

G A Nevinsky, O I Lavrik, O O Favorova, L L Kisselev.   

Abstract

A simple and rapid column procedure is described for the isolation from protein hydrolysates of peptides containing covalently bound substrate analogues with cis-diol groups. The method is based on complex formation between the cis-diol groups of peptide-bound compounds and dihydroxyborylic groups of a dihydroxyborylaminoethyl cellulose column. The method is useful for isolation of peptide(s) located in or near the active centre of enzymes after their affinity labelling by chemically active analogues of natural substrates like ribonucleotides, sugars, etc.

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Year:  1978        PMID: 368598     DOI: 10.1007/bf00777521

Source DB:  PubMed          Journal:  Mol Biol Rep        ISSN: 0301-4851            Impact factor:   2.316


  8 in total

1.  Affinity labelling of tryptophanyl-transfer RNA synthetase.

Authors:  V Z Akhverdyan; L L Kisselev
Journal:  J Mol Biol       Date:  1977-07-05       Impact factor: 5.469

2.  Investigation of the phenylalanyl-tRNA synthetase modification with gamma-(p-azidoanilide-)-ATP.

Authors:  V N Ankilova; D G Knorre; V V Kravchenko; O I Lavrik; G A Nevinsky
Journal:  FEBS Lett       Date:  1975-12-01       Impact factor: 4.124

3.  Direct and specific photochemical cross-linking of adenosine 5'-triphosphate to an aminoacyl-tRNA synthetase.

Authors:  V T Yue; P R Schimmel
Journal:  Biochemistry       Date:  1977-10-18       Impact factor: 3.162

4.  The subunit structure of phenylalanyl-tRNA synethetase of Escherichia coli.

Authors:  M H Kosakowski; A Böck
Journal:  Eur J Biochem       Date:  1970-01

5.  The isolation and properties of phenylalanyl ribonucleic acid synthetase from Escherichia coli B.

Authors:  M P Stulberg
Journal:  J Biol Chem       Date:  1967-03-10       Impact factor: 5.157

6.  Synthesis of cellulose derivatives containing the dihydroxyboryl group and a study of their capacity to form specific complexes with sugars and nucleic acid components.

Authors:  H L Weith; J L Wiebers; P T Gilham
Journal:  Biochemistry       Date:  1970-10-27       Impact factor: 3.162

7.  An improved method for the purification of tRNA by chromatography on dihydroxyboryl substituted cellulose.

Authors:  T F McCutchan; P T Gilham; D Söll
Journal:  Nucleic Acids Res       Date:  1975-06       Impact factor: 16.971

8.  Labelling of L-isoleucine tRNA ligase from Escherichia coli with L-isoleucyl-bromomethyl ketone.

Authors:  P Rainey; E Holler; M R Kula
Journal:  Eur J Biochem       Date:  1976-04-01
  8 in total

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