Isolation and characterization of a basic keratin-like protein from mammalian spermatozoa
| Autor: | D.T. Mayer, D.M. Henricks |
|---|---|
| Rok vydání: | 1965 |
| Předmět: |
Electrophoresis
Male Chemical Phenomena Arginine Swine Polyacrylamide Ion chromatography Cystine In Vitro Techniques Biology chemistry.chemical_compound Residue (chemistry) medicine Animals Amino Acids Mercaptoethanol Spermatozoon Proteins Cell Biology Chromatography Ion Exchange Spermatozoa Chemistry medicine.anatomical_structure chemistry Biochemistry Keratins Cattle Basic keratin |
| Zdroj: | Experimental Cell Research. 40:402-412 |
| ISSN: | 0014-4827 |
| DOI: | 10.1016/0014-4827(65)90273-9 |
| Popis: | A study incorporating amino acid analysis by ion exchange chromatography and polyacrylamide electrophoresis of two species of mammalian spermatozoa was conducted. The results indicate that a substantial structure of basic keratin is located within the spermatozoon. Disrupting this structure by treatment with various concentrations of mercaptoethanol gave two fractions of interest: an acid-soluble protein containing over 30 per cent arginine and 4 per cent half-cystine, and a residue which contained over 25 per cent arginine and 5–8 per cent half-cystine. Increasing the mercaptoethanol concentration solubilized more of the residue. This solubilized material was richer in arginine and cystine than the less resistant material which went into solution more readily. |
| Databáze: | OpenAIRE |
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