Your browser doesn't support javascript.
loading
Show: 20 | 50 | 100
Results 1 - 1 de 1
Filter
Add more filters










Database
Language
Publication year range
1.
Biochim Biophys Acta ; 1293(2): 272-6, 1996 Apr 16.
Article in English | MEDLINE | ID: mdl-8620040

ABSTRACT

We extracted proteins from the organic matrix of calcareous concretions, which represents the calcium storage form in a terrestrial crustacean. Electrophoretic analyses of water-soluble organic-matrix proteinaceous components revealed 11 polypeptides, 6 of which are probably glycosylated. Among the unglycosylated proteins, we characterized a 23 kDa polypeptide, with an isoelectric point of 5.5, which is able to bind calcium. Its N-terminal sequence is rich in acidic amino acids (essentially aspartic acid). All these characteristics suggest its involvement in the calcium precipitation process within the successive layers of the organic matrix.


Subject(s)
Calcium-Binding Proteins/chemistry , Calcium/metabolism , Crustacea/chemistry , Amino Acid Sequence , Animals , Aspartic Acid/chemistry , Calcium-Binding Proteins/metabolism , Electrophoresis, Gel, Two-Dimensional , Electrophoresis, Polyacrylamide Gel , Glycopeptides/chemistry , Male , Molecular Sequence Data , Molting , Peptides/chemistry , Peptides/metabolism
SELECTION OF CITATIONS
SEARCH DETAIL
...