Literature DB >> 6824676

Isolation and physico-chemical properties of blood platelet alpha-actinin.

F Landon, A Olomucki.   

Abstract

A procedure for the isolation of alpha-actinin from human blood platelets is described. Typical yields were 10-13 mg from 48 g of frozen platelets. The purified platelet alpha-actinin has many physico-chemical properties (molecular weight in native state, molecular weight in denaturing conditions, Stokes radius, ellipticities at 208 and 221 nm) similar to those of muscle alpha-actinins. However, in contrast to muscle alpha-actinins, it is composed of isoforms containing subunits of slightly different molecular weights and its effect on actin gelation is calcium-sensitive. These two characteristics are common to other known non-muscle alpha-actinins.

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Year:  1983        PMID: 6824676     DOI: 10.1016/0167-4838(83)90368-0

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN: 0006-3002


  4 in total

1.  Cation effects on the conformations of muscle and non-muscle alpha-actinins.

Authors:  E F Wenegieme; A P Naren; J A Bobich
Journal:  Biometals       Date:  1996-07       Impact factor: 2.949

2.  Proteins of the human placental microvillar cytoskeleton. alpha-Actinin.

Authors:  O A Vanderpuye; H C Edwards; A G Booth
Journal:  Biochem J       Date:  1986-01-15       Impact factor: 3.857

3.  Alpha-actinin synthesis can be modulated by antisense probes and is autoregulated in non-muscle cells.

Authors:  H Schulze; A Huckriede; A A Noegel; M Schleicher; B M Jockusch
Journal:  EMBO J       Date:  1989-12-01       Impact factor: 11.598

4.  Calcium-sensitive, lipid-binding cytoskeletal proteins of the human placental microvillar region.

Authors:  H C Edwards; A G Booth
Journal:  J Cell Biol       Date:  1987-07       Impact factor: 10.539

  4 in total

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