Novel Ca2+-activated neutral protease from an aquatic fungus, Allomyces arbuscula
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چکیده
منابع مشابه
Novel Ca2+-activated neutral protease from an aquatic fungus, Allomyces arbuscula.
A Ca2+-activated neutral protease was purified to homogeneity from an aquatic Phycomycete fungus, Allomyces arbuscula. It requires millimolar concentrations of Ca2+ for activation (1.8 to 2 mM for 50% activation). Sr2+ can replace Ca2+ but at higher concentrations (4 mM for 50% activation). The enzyme is a dimer of 40-kilodalton subunits and contains six cysteine residues, three of which are re...
متن کاملPurification and characterization of two forms of Ca2+-activated neutral protease from calf brain.
Two forms (CANP1 and CANP2) of a calcium-activated neutral protease (CANP) have been purified, 1,950- and 1,250-fold, respectively, to near homogeneity from calf brain. The purification procedure involves ammonium sulfate fractionation of the brain cytosol followed by chromatography on DEAE-Sephacel, hydroxylapatite, and alpha-casein-CH-Sepharose 4B affinity gel. A protein with apparent Mr = 17...
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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...
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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 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...
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ژورنال
عنوان ژورنال: Journal of Bacteriology
سال: 1988
ISSN: 0021-9193,1098-5530
DOI: 10.1128/jb.170.3.1254-1260.1988