Autor: |
Humphrey, G. F., Webster, H. L. |
Zdroj: |
Australian Journal of Experimental Biology & Medical Science; Jan1951, Vol. 29 Issue 1, p17-21, 5p, 4 Charts, 1 Graph |
Abstrakt: |
The QNH3 (µ1. NH3/mg. dry wt./hr.) for the deamination of adenylic acid by myosin gel is of the order of 1,000 to 1,500; with recrystallized myosin the value is about 2,500. Deamination is most rapid at pH 5-5 and is accelerated in the presence of 0-01 M CaCl2 or MgCl2. Reagents such as iodoacetate, iodosobenzoate and phenylmercuricacetate inhibit deamination; the activity of preparations which have aged, can be stimulated by glutathione. Adenylic acid does not affect the ability of myosin to dephosphorylate ATP. ADP- and ATP-protins stimulate adenylic acid deaminase activity of myosin gel, but not recrystallized myosin; it is concluded that crystalline myosin retains its structural integrity more easily than myosin gel. [ABSTRACT FROM AUTHOR] |
Databáze: |
Complementary Index |
Externí odkaz: |
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