Purification and characterisation of phosphorylase from muscle of Tilapia(Tipapia mosambica)
Purification and characterisation of phosphorylase from muscle of Tilapia(Tipapia mosambica)
| dc.contributor.author | Mukundan, M.K.. | |
| dc.contributor.author | Nair, M.R. | |
| dc.date.accessioned | 2017-08-11T06:25:56Z | |
| dc.date.available | 2017-08-11T06:25:56Z | |
| dc.date.issued | 1977 | |
| dc.description.abstract | Phosphorylase from muscle of tilapia (Tilapia mosambica) was extracted by water and purified by ammonium sulphate precipitation, centrifugation and repeated recrystallisation. Electrephorogram of the enzyme preparation showed a single band near origin. The enzyme showed optimum pH and temperature at 6.1 and 37°C respectively. Glucose and glucose-6-phosphate were found to be competitive inhibitors of the enzyme. Maltose and starch acted as primers for the phosphorylase reaction like glycogen.02 | en_US |
| dc.identifier.citation | Fish Technol.14(1):1-6 | en_US |
| dc.identifier.uri | http://hdl.handle.net/123456789/2850 | |
| dc.language.iso | en | en_US |
| dc.publisher | Society of Fisheries Technologis(India) | en_US |
| dc.title | Purification and characterisation of phosphorylase from muscle of Tilapia(Tipapia mosambica) | en_US |
| dc.type | Article | en_US |
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