Abstract
1. Rat intestinal smooth muscle was shown to contain endogenous inhibitory activity towards the neutral trypsin-like muscle proteinase described previously [Beynon & Kay (1978) Biochem. J. 173, 291--298]. 2. Comtamination of the muscle tissue by mucosal, blood and pancreatic inhibitors was shown to be unlikely. 3. The inhibitory activity was resolved into high- and low-molecular-weight components. 4. The low-molecular-weight component was purified to homogeneity. It has a molecular weight of approx. 9000 and was stable over the pH range 3--11. 5. It inhibited the muscle proteinase competitively (Ki congruent to t microM), but had no effect on any of the other proteinases tested. 6. Leupeptin also inhibited the muscle proteinase competitively (Ki congruent to 0.3 microM), whereas the low-molecular weight proteins gastrin, glucagon and insulin B-chain had very little effect. 7. A role for a weakly binding inhibitor in modulating the influence of the neutral proteinase on intracellular protein degradation is considered.
MeSH Terms
Amino Acids/analysis
Animals
Chromatography, Ion Exchange
Electrophoresis, Polyacrylamide Gel
Hydrolysis
Intestine, Small
Kinetics
Leupeptins/pharmacology
Malate Dehydrogenase/antagonists & inhibitors
Male
Molecular Weight
Muscle, Smooth/analysis
Peptides/pharmacology
Protease Inhibitors/isolation & purification,pharmacology
Proteins/pharmacology
Rats
Chemicals
Amino Acids
Leupeptins
Peptides
Protease Inhibitors
Proteins
Malate Dehydrogenase
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Carney I T
Curtis C G
Kay J K
Birket N
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