Isolation and amino-acid sequence analysis of human sperm protamines P1 and P2. Occurrence of two forms of protamine P2
| Autor: | Hubert Ammer, Agnes Henschen, Chul-Hoon Lee |
|---|---|
| Rok vydání: | 1986 |
| Předmět: |
chemistry.chemical_classification
Male biology Thermolysin Metalloendopeptidases Cleavage (embryo) Biochemistry Protamine Sperm Spermatozoa Amino acid chemistry.chemical_compound chemistry Endopeptidases biology.protein Humans Cyanogen bromide Amino Acid Sequence Cyanogen Bromide Protamines Guanidine Chromatography High Pressure Liquid Cysteine |
| Zdroj: | Biological chemistry Hoppe-Seyler. 367(6) |
| ISSN: | 0177-3593 |
| Popis: | The two protamines of human sperm cell nuclei, P1 and P2, were isolated in pure form after extraction with 6M guanidine/5% mercaptoethanol and alkylation with vinyl pyridine by reversed-phase high-performance liquid chromatography. The amino-acid sequence of protamine P1 was determined by analysing the intact protein and the fragments obtained by cyanogen bromide cleavage. Out of the 50 amino-acid residues 24 are arginines and 6 are cysteines. The sequence of protamine P2 was determined by analysing the intact protein and the fragments resulting from cleavage with endoproteinase Lys-C and thermolysin. Protamine P2 was found to occur in two forms which only differ in their N-terminal regions. The form P2' is three amino-acid residues longer at the N-terminus than the form P2''. Out of the 57 amino-acid residues in the longer form 27 are arginines and 5 are cysteines. Human protamine P1 is highly homologous with the protamines isolated from bull, boar, ram and mouse sperm cells, but human protamine P2 shows a novel type of structure, although also here the dominant amino acids are arginine and cysteine. |
| Databáze: | OpenAIRE |
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