scholarly journals Purification and properties of a catalytically active fragment of soluble nucleoside triphosphatase from bovine kidney

2013 ◽  
Vol 85 (3) ◽  
pp. 31-37
Author(s):  
А. F. Makarchikov ◽  
Keyword(s):  
Bovine Kidney ◽  
Purification And Properties ◽  
Catalytically Active ◽  
Active Fragment ◽  
Nucleoside Triphosphatase

scholarly journals Purification and properties of 2-aminoadipate: 2-oxoglutarate aminotransferase from bovine kidney

1989 ◽  
Vol 261 (3) ◽  
pp. 761-768 ◽  
Author(s):  
D R Deshmukh ◽  
S M Mungre
Keyword(s):  
Rat Kidney ◽  
Deae Cellulose ◽  
Dicarboxylic Acids ◽  
Structural Similarity ◽  
Appreciable Amount ◽  
Kinetic Properties ◽  
Bovine Kidney ◽  
Purification And Properties ◽  
Kidney Enzyme ◽  
Structural Differences

Previous studies with rat kidney preparations indicated that 2-aminoadipate aminotransferase (AadAT) and kynurenine aminotransferase (KAT) activities are properties of a single protein. We found that bovine kidney contains an appreciable amount of AadAT activity, but lacks KAT activity. AadAT from bovine and rat kidney extracts were purified to electrophoretic homogeneity. The purification procedure included fractionation with (NH1)2SO1, heat treatment, DEAE-cellulose chromatography and hydroxyapatite chromatography. Physical and kinetic properties, such as pH optima, Km for substrates, Mr, electrophoretic mobility and inhibition by dicarboxylic acids of bovine kidney AadAT, were similar to those of the rat kidney enzyme. However, bovine kidney AadAT differed from rat kidney AadAT in substrate specificity, amino acid composition and stability when stored. The titration curve of bovine kidney AadAT was also different from that of the rat kidney enzyme. The results suggest that bovine kidney AadAT may have some structural similarity to rat kidney AadAT and that the structural differences observed between the two enzymes may explain the absence of KAT activity in bovine kidney.

scholarly journals Proteolytic release of keratinocyte transglutaminase

1990 ◽  
Vol 265 (2) ◽  
pp. 351-357 ◽  
Author(s):  
R H Rice ◽  
X Rong ◽  
R Chakravarty
Keyword(s):  
Fatty Acid ◽  
Cultured Cells ◽  
Limited Proteolysis ◽  
Terminal Differentiation ◽  
Human Keratinocytes ◽  
Post Translational Modification ◽  
Catalytically Active ◽  
Endogenous Release ◽  
Acid Esterification ◽  
Active Fragment

Human keratinocytes express a particulate transglutaminase that can be released from the membrane by limited proteolysis with trypsin or plasmin to yield a form that is congruent to 80 kDa. The enzyme from cultured cells was also releasable by endogenous proteolysis to yield a catalytically active fragment of congruent to 80 kDa. Endogenous release was strongly dependent upon temperature and Ca2+ concentration and was inhibited by iodoacetate, but not by leupeptin, antipain or phenylmethanesulphonyl fluoride. These phenomena raise the possibility of partial translocation of transglutaminase activity to the cytoplasm by proteolysis to which the enzyme is subject during terminal differentiation. In addition, hydrodynamic measurements showed that the endogenously released enzyme was monomeric in solution (79 kDa), whereas that solubilized by hydroxylamine without proteolysis appeared dimeric (190 kDa). The latter dimeric state may reflect either an altered conformation of the enzyme or post-translational modification beyond fatty acid esterification.

Purification and Properties of Bovine Kidney Ribonucleases

1985 ◽  
Vol 97 (3) ◽  
pp. 923-934 ◽  
Author(s):  
Yasushi NIWATA ◽  
Kazuko OHGI ◽  
Akihiro SANDA ◽  
Yoshio TAKIZAWA ◽  
Masachika IRIE
Keyword(s):  
Bovine Kidney ◽  
Purification And Properties
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