Calcium activated neutral protease. - Structure-function relationship and functional implications.
نویسندگان
چکیده
منابع مشابه
[Activation mechanism of calcium-activated neutral protease].
The activation mechanism through limited autolysis of a calcium-activated neutral protease (CANP) with a high sensitivity to calcium ions (pCANP) was analyzed. The rate of autolysis was dependent on pCANP concentration. The reaction was inhibited by high concentrations of digestible substrates but not by a nondigestible substrate. Incubation of pCANP inactivated by Nethylmaleimide with a small ...
متن کاملCalcium activated neutral protease from human skeletal muscle.
Koichi SUZUKI, Shoichi ISHIURA*, Shuichi TSUTI, Tetsuo KATAMOTO, Hideo SUGITA*p** and Kazutomo IMAHORI Department of Biochemistry, Faculty of Med&ine, University of Tokyo, Bunkyo-ku, Tokyo, Japan; *Division of Neu~muscu~r Research, Nat~~t Center for Nervous, rental, and Tuscan Disorders, Kodaira, Tokyo, Japan; and **De~r~~t of Ne~io~, Insti~te of Brain Research, Faculty of medicine, ~niversi~ o...
متن کاملProteolytic activation of calcium-activated, phospholipid-dependent protein kinase by calcium-dependent neutral protease.
A Ca2+-dependent protease I), which hydrolyzes casein at Ca2+ concentrations lower than the 10(-5) M range, is purified roughly 4000-fold from the soluble fraction of rat brain. This protease is able to activate Ca2+-activated, phospholipid-dependent protein kinase (protein kinase C) by limited proteolysis analogously to the previously known Ca2+-dependent analogously to the previously known Ca...
متن کاملProperties of erythrocyte membrane binding and autolytic activation of calcium-activated neutral protease.
The binding of a calcium-activated neutral protease (CANP) with high calcium sensitivity (muCANP) to erythrocyte membranes and its subsequent autolytic activation on the membranes were analyzed by an immunoblot technique. In the presence of calcium ions, muCANP bound to the erythrocyte membranes as a heterodimer of 79- and 28-kDa subunits and was converted quickly on the membranes to an active ...
متن کاملRemoval of Z-lines and alpha-actinin from isolated myofibrils by a calcium-activated neutral protease.
A calcium-activated factor (CaAF) has been isolated and partially purified from the post-myofibrillar supernatant fraction of rabbit skeletal muscle. The 200-fold purified CaAF hydrolyzed denatured casein, [3-H]acetyl hemoglobin, and N-ethyl[3-H]maleimide-labeled alpha-actinin. The proteolytic activity has a pH optimum at 6.9 and is dependent on the presence of Ca2+ (optimum concentration, 10 m...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Cell Structure and Function
سال: 1990
ISSN: 0386-7196,1347-3700
DOI: 10.1247/csf.15.1