Literature DB >> 7141076

The structure of Artemia sp. haemoglobins-I. Isolation and characterization of oxygen binding domains obtained by limited tryptic digestion.

D Geelen, L Moens, J Heip, R Hertsens, K Donceel, J Clauwaert.   

Abstract

Limited tryptic digestion of the extracellular haemoglobins of the crustacea Artemia sp. result in series of discrete fragments which are multiples of 16,000 d. 2. These 16,000 d fragments, together with 50,000 d and 80,000 d fragments have similar amino acid composition and tryptic peptide maps as the intact globin chains. 3. The haem content of the 16,000 d fragments is the same as this of the intact pigment and they can bind oxygen in a non cooperative way. 4. These results strongly support that the 16,000 d fragments represent structural and functional units or domains from which the globin chains are built up.

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Year:  1982        PMID: 7141076     DOI: 10.1016/0020-711x(82)90060-x

Source DB:  PubMed          Journal:  Int J Biochem        ISSN: 0020-711X


  2 in total

1.  The structure of Artemia sp. (brine shrimp) haemoglobins. Purification of a structural unit to homogeneity.

Authors:  L Moens; M L Van Hauwaert; G Wolf
Journal:  Biochem J       Date:  1985-05-01       Impact factor: 3.857

2.  The structure of Artemia sp. haemoglobin. Cleavage of the native molecules into functional units by limited subtilisin digestion.

Authors:  L Moens; D Geelen; M L Van Hauwaert; G Wolf; R Blust; R Witters; R Lontie
Journal:  Biochem J       Date:  1984-11-01       Impact factor: 3.857

  2 in total

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