Literature DB >> 6750594

Identification and characterization of a calcium-binding protein from human placenta.

R S Tuan.   

Abstract

The human placenta has been found to contain a specific calcium-binding protein (HCaBP) which increases in amount as a function of gestation. A procedure is described for the purification of the HCaBP to chromatographic and electrophoretic homogeneity. The HCaBP is (a) a high molecular weight protein with a native Mr of 150 000 and appears to be a dimer of subunits of Mr = 70 000; and (b) an acidic protein with a pI of 4.6. Amino acid analysis of the HCaBP revealed an abundance of acidic amino acid residues (27 per cent = Asp and Glu). A specific antiserum has been prepared against purified HCaBP. With Ouchterlony double immunodiffusion, the HCaBP appears to be specific for the human placenta, and is not cross-immunoreactive with the CaBP of the chick embryonic chorio-allantoic membrane.

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Year:  1982        PMID: 6750594     DOI: 10.1016/s0143-4004(82)80048-9

Source DB:  PubMed          Journal:  Placenta        ISSN: 0143-4004            Impact factor:   3.481


  3 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.  Ca2+-binding protein of the human placenta. Characterization, immunohistochemical localization and functional involvement in Ca2+ transport.

Authors:  R S Tuan
Journal:  Biochem J       Date:  1985-04-01       Impact factor: 3.857

3.  Identification and characterization of a calcium-binding protein in the mouse chorioallantoic placenta.

Authors:  R S Tuan; S T Cavanaugh
Journal:  Biochem J       Date:  1986-01-01       Impact factor: 3.857

  3 in total

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