| Autor: |
Epstein E, Baginski ES, Zak B |
| Jazyk: |
angličtina |
| Zdroj: |
Annals of clinical and laboratory science [Ann Clin Lab Sci] 1978 Jan-Feb; Vol. 8 (1), pp. 34-41. |
| Abstrakt: |
A procedure has been described whereby the high molecular weight alkaline phosphatase (slow-moving) isoenzyme may be studied by means of polyacrylamide gel electrophoresis. By treatment of sera containing this isoenzyme with some detergents of the nonionic Triton octylphenoxyethanol series, the high molecular weight alkaline phosphatase isoenzyme is altered so that its electrophoretic mobility more closely resembles that of the usual alklaine phosphatase isoenzymes. The high molecular weight isoenzyme is thought to be associated with phosphatidyl choline and/or liproproteins. The detergent action is to dissociated the alkaline phosphatase from its lipid carrier. It is thought that these lipid-alkaline phosphatase complexes are associated with liver cell fragments. The detergent altered slow-moving alkaline phosphatase may migrate as a single band, from two to four new bands, or as several new bands. Liver, bone and intestinal alkaline phosphatase isoenzymes are unaffected by detergent action. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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