Different Tissue Distributions of Two Types of Thiol Proteinase Inhibitors from Rat Liver and Epidermis1

1984 ◽  
Vol 96 (5) ◽  
pp. 1437-1442 ◽  
Author(s):  
Eiki KOMINAMI ◽  
Yoshiaki BANDO ◽  
Nobuaki WAKAMATSU ◽  
Nobuhiko KATUNUMA
Keyword(s):  
Rat Liver ◽  
Proteinase Inhibitors ◽  
Thiol Proteinase

scholarly journals A new thiol proteinase from rat liver.

1981 ◽  
Vol 256 (5) ◽  
pp. 2567-2572
Author(s):  
E. Gohda ◽  
H.C. Pitot
Keyword(s):  
Rat Liver ◽  
Thiol Proteinase

scholarly journals Proteolytic activation and solubilization of endoplasmic-reticulum cyclic AMP phosphodiesterase activity

1983 ◽  
Vol 213 (1) ◽  
pp. 99-105 ◽  
Author(s):  
S R Wilson ◽  
M D Houslay
Keyword(s):  
Endoplasmic Reticulum ◽  
Proteinase Inhibitors ◽  
Smooth Endoplasmic Reticulum ◽  
Limited Proteolysis ◽  
Proteolytic Activation ◽  
Freeze Thaw ◽  
Membrane Bound ◽  
Time Courses ◽  
Triton X ◽  
Thiol Proteinase

Dithiothreitol led to the activation and solubilization of the cyclic nucleotide phosphodiesterase activities associated with the smooth and various rough subfractions of rat liver endoplasmic reticulum. The activity in each of the subfractions exhibited somewhat different time courses, and sensitivities to dithiothreitol concentration, in respect of their solubilization and activation. Both activation and solubilization by dithiothreitol could be blocked by either thiol proteinase inhibitors or excess bovine serum albumin. Freeze-thaw solubilization was not blocked by the thiol proteinase inhibitor antipain and did not lead to the activation of the enzyme. After dithiothreitol-induced solubilization, all of the enzymes exhibited non-linear Lineweaver-Burk plots indicative of apparent negative co-operativity. In contrast, after freeze-thaw solubilization the enzyme in the smooth-endoplasmic-reticulum-plus-Golgi fraction still obeys Michaelis kinetics, as does the membrane-bound enzyme. It is possible to mimic the action of dithiothreitol in solubilizing and activating the enzyme by limited proteolysis with trypsin. Triton X-100 is highly efficient at solubilizing these enzymes, yet has little effect on their activities. Charged detergents exhibit highly selective effects on the enzymes as regards their solubilization and activity expressed.

Studies on thiol proteinase inhibitors in rat peripheral blood cells

1984 ◽  
Vol 123 (2) ◽  
pp. 816-821 ◽  
Author(s):  
Eiki Kominami ◽  
Toshifumi Tsukahara ◽  
Kunio Ii ◽  
Kazuo Hizawa ◽  
Nobuhiko Katunuma
Keyword(s):  
Peripheral Blood ◽  
Blood Cells ◽  
Proteinase Inhibitors ◽  
Peripheral Blood Cells ◽  
Thiol Proteinase
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