Subunit structured of pig small-intestinal brush-border aminopeptidase N
| Autor: | A Benajiba, S Maroux |
|---|---|
| Rok vydání: | 1981 |
| Předmět: |
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Swine Protein subunit Proteolysis Peptide CD13 Antigens Biology Cleavage (embryo) Aminopeptidases Biochemistry Intestine Small medicine Animals Peptide bond Amino Acids Molecular Biology chemistry.chemical_classification Microvilli medicine.diagnostic_test Cell Biology Molecular biology Peptide Fragments Amino acid Molecular Weight Enzyme chemistry Chromatography Gel Electrophoresis Polyacrylamide Gel Research Article |
| Zdroj: | Biochemical Journal. 197:573-580 |
| ISSN: | 0264-6021 |
| DOI: | 10.1042/bj1970573 |
| Popis: | Aminopeptidase N (EC 3.4.11.2), when isolated from pig intestine in either the proteinase- or detergent-released form, frequently appears to contain three polypeptide chains, here termed alpha, beta and gamma. We have established by an immunological technique that the beta- and gamma-polypeptides are derived from the alpha-chain and that the intact enzyme is a dimer, alpha 2. Each alpha-chain of the detergent form was shown to contain a hydrophobic anchor peptide about 35 amino acid residues in length, which included the N-terminal sequences. A peptide bond in the alpha-chain was very sensitive to proteolysis. Its cleavage generated the commonly observed forms: alpha beta gamma and beta 2 gamma 2. The gamma-fragment, which lacked the anchor peptide, was derived from the C-terminal part of the alpha-chain. |
| Databáze: | OpenAIRE |
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