On cholinesterase activity and some physicochemical properties of fractions prepared from heat-treated myosin solutions
| ISSN: |
0003-9861
|
|---|---|
| Source: |
Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
|
| Topics: |
Biology
Chemistry and Pharmacology
Physics
|
| Type of Medium: |
Electronic Resource
|
| URL: |
| _version_ | 1798292182933700608 |
|---|---|
| autor | Kover, A. Szoor, A. Szabolcs, M. |
| autorsonst | Kover, A. Szoor, A. Szabolcs, M. |
| book_url | http://dx.doi.org/10.1016/0003-9861(64)90294-2 |
| datenlieferant | nat_lic_papers |
| fussnote | A cholinesterase fraction (S"1) having a sedimentation coefficient of 2.9 S was found to be released from myosin solution by a heat treatment carried out at 53 ^o and pH 6.2 for 5 minutes. It could be resolved by dialyzing into a P"1-fraction of 3.76 S precipitating at a low ionic strength, and a D"1-fraction of 1.45 S remaining in solution under the same conditions. The cholinesterase activity has mainly passed into the P"1-fraction or, after its heat treatment, into the P"2-fraction. The specific activities of the P"1 and P"2 fractions were much more higher (55 and 120 μg acetylcholine (ACh) per milligram protein per hour, respectively) than that of the original myosin solution (8-10 μg Ach/mg prot./hour) or D"1-fraction (5-6 μg ACh per milligram protein per hour).If previous to heat treatment a short tryptic digestion was applied, the properties of heat-supernatant (S"1) principally changed as at reducing of its ionic strength by dialyzing, the great part of its protein content and cholinesterase activity was obtained in the D"1-fraction. In this case the specific activity of the D"1-fraction was considerably more (50 μg Ach/mg prot./hour) than that of the P"1-fraction (17 μg Ach/mg prot./hour). |
| hauptsatz | hsatz_simple |
| identnr | NLZ183913698 |
| issn | 0003-9861 |
| journal_name | Archives of Biochemistry and Biophysics |
| materialart | 1 |
| package_name | Elsevier |
| publikationsort | Amsterdam |
| publisher | Elsevier |
| reference | 107 (1964), S. 382-387 |
| search_space | articles |
| shingle_author_1 | Kover, A. Szoor, A. Szabolcs, M. |
| shingle_author_2 | Kover, A. Szoor, A. Szabolcs, M. |
| shingle_author_3 | Kover, A. Szoor, A. Szabolcs, M. |
| shingle_author_4 | Kover, A. Szoor, A. Szabolcs, M. |
| shingle_catch_all_1 | Kover, A. Szoor, A. Szabolcs, M. On cholinesterase activity and some physicochemical properties of fractions prepared from heat-treated myosin solutions 0003-9861 00039861 Elsevier |
| shingle_catch_all_2 | Kover, A. Szoor, A. Szabolcs, M. On cholinesterase activity and some physicochemical properties of fractions prepared from heat-treated myosin solutions 0003-9861 00039861 Elsevier |
| shingle_catch_all_3 | Kover, A. Szoor, A. Szabolcs, M. On cholinesterase activity and some physicochemical properties of fractions prepared from heat-treated myosin solutions 0003-9861 00039861 Elsevier |
| shingle_catch_all_4 | Kover, A. Szoor, A. Szabolcs, M. On cholinesterase activity and some physicochemical properties of fractions prepared from heat-treated myosin solutions 0003-9861 00039861 Elsevier |
| shingle_title_1 | On cholinesterase activity and some physicochemical properties of fractions prepared from heat-treated myosin solutions |
| shingle_title_2 | On cholinesterase activity and some physicochemical properties of fractions prepared from heat-treated myosin solutions |
| shingle_title_3 | On cholinesterase activity and some physicochemical properties of fractions prepared from heat-treated myosin solutions |
| shingle_title_4 | On cholinesterase activity and some physicochemical properties of fractions prepared from heat-treated myosin solutions |
| sigel_instance_filter | dkfz geomar wilbert ipn albert fhp |
| source_archive | Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 |
| timestamp | 2024-05-06T08:44:28.167Z |
| titel | On cholinesterase activity and some physicochemical properties of fractions prepared from heat-treated myosin solutions |
| titel_suche | On cholinesterase activity and some physicochemical properties of fractions prepared from heat-treated myosin solutions A cholinesterase fraction (S"1) having a sedimentation coefficient of 2.9 S was found to be released from myosin solution by a heat treatment carried out at 53 ^o and pH 6.2 for 5 minutes. It could be resolved by dialyzing into a P"1-fraction of 3.76 S precipitating at a low ionic strength, and a D"1-fraction of 1.45 S remaining in solution under the same conditions. The cholinesterase activity has mainly passed into the P"1-fraction or, after its heat treatment, into the P"2-fraction. The specific activities of the P"1 and P"2 fractions were much more higher (55 and 120 μg acetylcholine (ACh) per milligram protein per hour, respectively) than that of the original myosin solution (8-10 μg Ach/mg prot./hour) or D"1-fraction (5-6 μg ACh per milligram protein per hour).If previous to heat treatment a short tryptic digestion was applied, the properties of heat-supernatant (S"1) principally changed as at reducing of its ionic strength by dialyzing, the great part of its protein content and cholinesterase activity was obtained in the D"1-fraction. In this case the specific activity of the D"1-fraction was considerably more (50 μg Ach/mg prot./hour) than that of the P"1-fraction (17 μg Ach/mg prot./hour). |
| topic | W V U |
| uid | nat_lic_papers_NLZ183913698 |