Panulirus interruptus hemocyanin. The amino acid sequence of subunit b and anomalous behaviour of subunits a and b on polyacrylamide gel electrophoresis in the presence of SDS
| Autor: | Peter A. Jekel, Jaap J. Beintema, Nell M. Soeter, Henk J. Bak, Johan M. Vereijken |
|---|---|
| Rok vydání: | 1988 |
| Předmět: |
Gel electrophoresis
chemistry.chemical_classification Hydrolysis medicine.medical_treatment Protein subunit Molecular Sequence Data Protein primary structure Hemocyanin Trypsin Biochemistry Peptide Fragments Nephropidae Amino acid chemistry Hemocyanins medicine Animals Electrophoresis Polyacrylamide Gel Amino Acid Sequence Cyanogen Bromide Polyacrylamide gel electrophoresis Peptide sequence medicine.drug |
| Zdroj: | European Journal of Biochemistry. 178:403-412 |
| ISSN: | 1432-1033 0014-2956 |
| DOI: | 10.1111/j.1432-1033.1988.tb14464.x |
| Popis: | The primary structure of subunit b of Panulirus interruptus hemocyanin has been derived from two digests (trypsin and CNBr) and, in some cases, with aid from the similarity with the sequence of subunit a. Differences between the amidation states of Asx and Glx residues in subunit b relative to a were investigated more thoroughly. When compared to the sequence of subunit a, 18 differences (2.7%) were found and certain heterogeneities, indicating the presence of a minor subunit b', were observed. Several differences in properties between subunits a and b, including their anomalous behaviour on SDS/polyacrylamide gel electrophoresis, could be explained by amino acid replacements. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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