Endogenous protein kinase inhibitors. Purification, characterization, and distribution in different tissues.

Endogenous Protein Kinase Inhibitors

A thermostable inhibition of ATP:protein phosphotransferase (EC 2.7.1.37) (protein kinase) which is present in crude tissue extracts has been resolved by gel chromatography (Sephadex G-100) into two molecular forms. These two forms will be referred to as type I and type II inhibitor. The type I inhibitor (M, = 24,000) is specific for CAMP-dependent protein kinase and corresponds to the inhibito...

Protein purification from whole tissues . Fatemeh Mehrpooyan*

Purification and characterization of antiviral protein from silkworm fecal matter

Antiviral proteins (AVP), present in silkworm fecal matter, show activity against nuclear polyhedrosis virus (NPV) in vitro and in vivo. The extract of silkworm fecal matter prepared in phosphate buffer solution of pH 7.5 was subjected to 50% solid ammonium sulfate precipitation to enrich AVP, then which was dialyzed. The dialysate was applied to the column containing silica gel-G, the column e...

Purification and characterization of a wheat germ protein kinase.

A cyclic AMP-independent protein kinase has been purified from wheat germ extracts. The enzyme catalyzes the phosphorylation of casein and phosvitin but not protamine, histone, or bovine serum albumin. However, the best substrate for the kinase appears to be that of an endogenous wheat germ protein. The kinase can utilize both ATP and GTP as phosphoryl donors. A molecular weight of 36,000-38,00...

Expression, Purification, and Characterization of Protein Kinase C-r*

Of the recently described members of the protein kinase C (PKC) family (-6, -6, -c), no detailed properties of the purified enzymes have been presented. Here we describe the expression of PKC-c in insect cells using a baculovirus vector. The recombinant enzyme has been purified to homogeneity by sequential chromatography on DEAE-cellulose, serine-Sepharose, Mono Q, and Superose 12; the protein ...