scholarly journals Effect of Chronic Hypoxia on Oxidative Enzyme Activity in Rat Skeletal Muscle.

1993 ◽  
Vol 12 (6) ◽  
pp. 363-369 ◽  
Author(s):  
Hiromi TAKAHASHI ◽  
Kunio KIKUCHI ◽  
Hideaki NAKAYAMA
Keyword(s):  
Skeletal Muscle ◽  
Enzyme Activity ◽  
Chronic Hypoxia ◽  
Oxidative Enzyme ◽  
Rat Skeletal Muscle ◽  
Oxidative Enzyme Activity

scholarly journals The Comparison of Oxidative Enzyme Activity in Skeletal Muscle from Stroke-Prone Spontaneously Hypertensive and Normotensive Rats

1996 ◽  
Vol 37 (4) ◽  
pp. 579-579
Author(s):  
Shigehiko Ogoh ◽  
Sakiya Yamasaki ◽  
Hiroshi Okamoto ◽  
Satoshi Fukuda ◽  
Sadayoshi Taguchi
Keyword(s):  
Skeletal Muscle ◽  
Enzyme Activity ◽  
Oxidative Enzyme ◽  
Spontaneously Hypertensive ◽  
Oxidative Enzyme Activity

scholarly journals Identification and characterization of a tissue kallikrein in rat skeletal muscles

1987 ◽  
Vol 243 (3) ◽  
pp. 773-778 ◽  
Author(s):  
N Shimojo ◽  
J Chao ◽  
L Chao ◽  
H S Margolius ◽  
R K Mayfield
Keyword(s):  
Skeletal Muscle ◽  
Enzyme Activity ◽  
Skeletal Muscles ◽  
Proteinase Inhibitors ◽  
Oxidative Enzyme ◽  
Tissue Kallikrein ◽  
Urinary Kallikrein ◽  
Ph Optimum ◽  
Oxidative Enzyme Activity

A tissue kallikrein was purified from rat skeletal muscle. Characterization of the enzyme showed that it has alpha-N-tosyl-L-arginine methylesterase activity and releases kinin from purified bovine low-Mr kininogen substrate. The pH optimum (9.0) of its esterase activity and the profile of inhibition by serine-proteinase inhibitors are identical with those of purified RUK (rat urinary kallikrein). Skeletal-muscle kallikrein also behaved identically with urinary kallikrein in a radioimmunoassay using a polyclonal anti-RUK antiserum. On Western-blot analysis, rat muscle kallikrein was recognized by affinity-purified monoclonal anti-kallikrein antibody at a position similar to that of RUK (Mr 38,000). Immunoreactive-kallikrein levels were measured in skeletal muscles which have different fibre types. The soleus, a slow-contracting muscle with high mitochondrial oxidative-enzyme activity, had higher kallikrein content than did the extensor digitorum longus or gastrocnemius, both fast-contracting muscles with low oxidative-enzyme activity. Streptozotocin-induced diabetes reduced muscle weights, but did not alter the level of kallikrein (pg/mg of protein) in skeletal muscle, suggesting that insulin is not a regulator of kallikrein in this tissue. Although the role of kallikrein in skeletal muscle is unknown, its localization and activity in relation to muscle functions and disease can now be studied.

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