Literature DB >> 7353046

The purification of a unique calcium-binding protein from Morris hepatoma 5123 tc.

J P MacManus.   

Abstract

A heat-stable Ca2+-binding protein was purified to homogeneity from Morris hepatoma 5123 tc. It had an apparent molecular weight of 11 000, and isoelectric point of 3.9, and bound two atoms of calcium per molecule of protein. The spectral and amino acid analysis indicated the tumour protein to be similar to the parvalbumins. This protein has been shown to be absent in liver.

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Year:  1980        PMID: 7353046     DOI: 10.1016/0005-2795(80)90181-6

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


  4 in total

1.  The purification and complete amino acid sequence of the 9000-Mr Ca2+-binding protein from rat placenta. Identity with the vitamin D-dependent intestinal Ca2+-binding protein.

Authors:  J P MacManus; D C Watson; M Yaguchi
Journal:  Biochem J       Date:  1986-04-15       Impact factor: 3.857

2.  Conformational changes induced by binding of bivalent cations to oncomodulin, a paravalbumin-like tumour protein.

Authors:  J P MacManus; A G Szabo; R E Williams
Journal:  Biochem J       Date:  1984-05-15       Impact factor: 3.857

3.  Molar absorptivity and A 1% 1cm values for proteins at selected wavelengths of the visible and ultraviolet regions. XXIII.

Authors:  D M Kirschenbaum
Journal:  Appl Biochem Biotechnol       Date:  1984-04       Impact factor: 2.926

Review 4.  Ion binding to calmodulin. A comparison with other intracellular calcium-binding proteins.

Authors:  M C Kilhoffer; J Haiech; J G Demaille
Journal:  Mol Cell Biochem       Date:  1983       Impact factor: 3.396

  4 in total

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