Zobrazeno 1 - 10
of 158
pro vyhledávání: '"A E, Mirsky"'
Publikováno v:
American Journal of Obstetrics and Gynecology. 223:980
Autor:
A W, POLLISTER, A E, MIRSKY
Publikováno v:
The Anatomical record. 94
Autor:
I, SNAPPER, A E, MIRSKY
Publikováno v:
Blood. 2(4)
Autor:
M L, Anson, A E, Mirsky
Publikováno v:
The Journal of General Physiology
1. By a procedure involving the use of acid acetone hemoglobin may be rapidly separated into a precipitate of denatured globin and an acetone solution of heme. 2. By neutralization procedures the denatured globin may be largely converted into a solub
Autor:
M L, Anson, A E, Mirsky
Publikováno v:
The Journal of General Physiology
1. It is possible to prepare crystalline, soluble, heat-coagulable serum albumin from coagulated serum albumin. 2. In the cases so far studied, the more soluble a denatured protein, the more easily its denaturation can be reversed.
Autor:
Hans Ris, Alfred E. Mirsky
Publikováno v:
The Journal of General Physiology
By means of 1 M NaCl isolated lymphocyte chromosomes can be separated into two fractions, each of which contains nucleoprotein. The fraction soluble in M NaCl consists largely of desoxyribose nucleohistone, and constitutes 90 to 92 per cent of the ma
Autor:
A E, Cohn, A E, Mirsky
Publikováno v:
The Journal of General Physiology
We have studied by means of glass electrodes the hydrogen ion concentration of the blood of chicken embryos from 8 to 20 days. When plotted as a curve, the average data show that a constant change takes place in the measurement, being acid at the beg
Autor:
A E, Mirsky, M L, Anson
Publikováno v:
The Journal of General Physiology
Hemoglobin and the proteins of the crystalline lens contain active SH groups while in the native state, the number of active groups increasing as the pH rises. All the SH groups of denatured globin and of the denatured lens proteins are active at a p
Autor:
M. L. Anson, Alfred E. Mirsky
Publikováno v:
The Journal of General Physiology
There is a mobile equilibrium between the native and denatured forms of trypsin which depends on the concentrations of acid, alkali, and alcohol and on the temperature. The heat of denaturation in 0.01 N hydrochloric acid calculated from the effect o