Literature DB >> 3036147

Sequence homologies between p36, the substrate of pp60src tyrosine kinase and a 67 kDa protein isolated from bovine aorta.

F Martin, J Derancourt, J P Capony, S Colote, J C Cavadore.   

Abstract

A 67 kDa actin-binding protein was isolated from bovine aorta. Partial amino acid sequence determination of two large thermolysin peptides were used to compare 67 kDa bovine aorta protein and p36 the substrate of pp60src tyrosine kinase. Sequence analysis shows that 67 kDa bovine aorta protein shares common domains with p36 and possesses the consensus aminoacid sequences of mammalian Ca2+-dependent membrane-binding protein and p36/gelsolin.

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Year:  1987        PMID: 3036147     DOI: 10.1016/0006-291x(87)91059-x

Source DB:  PubMed          Journal:  Biochem Biophys Res Commun        ISSN: 0006-291X            Impact factor:   3.575


  3 in total

1.  Identification of the 32 kDa components of bovine lens EDTA-extractable protein as endonexins I and II.

Authors:  R Kobayashi; R Nakayama; A Ohta; F Sakai; S Sakuragi; Y Tashima
Journal:  Biochem J       Date:  1990-03-01       Impact factor: 3.857

2.  An immunological and biochemical comparison of 67 kDa calcimedin and 67 kDa calelectrin.

Authors:  R Kobayashi; Y Tashima
Journal:  Biochem J       Date:  1989-09-15       Impact factor: 3.857

3.  A 36 kDa monomeric protein and its complex with a 10 kDa protein both isolated from bovine aorta are calpactin-like proteins that differ in their Ca2+-dependent calmodulin-binding and actin-severing properties.

Authors:  F Martin; J Derancourt; J P Capony; A Watrin; J C Cavadore
Journal:  Biochem J       Date:  1988-05-01       Impact factor: 3.857

  3 in total

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