TY - JOUR
AU1 - Borćić, Olga
AU2 - Štraus, B.
AB -  Introduction Differences among arginases (,-arginine amidinohydrolase, EC 3.5.3.1) from various tissues were noted a long time ago when it was shown that the conditions for measuring arginase activity in one tissue were not equally suitable for arginase tests in another tissue (1). Differences in the pH activity curves (2) and immunochemical properties were also noted (3). Using electrophoretic (4) and Chromatographie techniques two isoenzymes of the mammary gland have been found (4, 5, 6), while the results concerning the number of liver and erythrocyte arginase isoenzymes are not consistent (4, 5, 6, 7, 8). This paper deals with the technique set up in our laboratory for the separation of arginase isoenzymes and with the results obtained with arginase from various human tissues. Material and Methods Tissues were obtained within six hours post mortem. They were washed with saline, freed of connective tissue and of fat which is particularly abundant in the mammary gland. Portions of Or 2 g of tissue were homogenized in z Potter Elvehjem hompgenizer in 1 ml of 5 g/1 Triton X-100 in 0.5 mmol/1 MnQ2 solution. The hpmpgenates were centrifuged at 14,000 g for 20 minutes the supernatants lypphilised and kept dry at + 
TI - Separation of Arginase Isoenzymes from Human Tissues by Agar Gel Electrophoresis
JF - Clinical Chemistry and Laboratory Medicine
DO - 10.1515/cclm.1976.14.1-12.533
DA - 1976-01-01
UR - https://www.deepdyve.com/lp/de-gruyter/separation-of-arginase-isoenzymes-from-human-tissues-by-agar-gel-HfDp5edgps
SP - 533
EP - 536
VL - 14
IS - 1-12
DP - DeepDyve