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Biomedical subjects

R J Pennington

Publications and source records attributed to R J Pennington.

At least 37 records · Page 2Linked to original sources
PubMed1979

Separation of cathepsin B1 and related enzymes from rat skeletal muscle.

Rat muscle was extracted at pH 4 and submitted to gel-filtration on Sephadex G-75 and to chromatography on DEAE-Sephadex. Gel-filtration gave a large peak of activity towards Bz-Arg-NNap with an estimated molecular weight of 25,500. Activity towards Bz-Arg-NH2 was present in this peak and in another peak of molecular weight 45,000. The second peak also hydrolysed benzoyl-glycyl-L-arginine. DEAE-Sephadex gave five peaks of Bz-Arg-NNap hydrolysing activity; all showed thiol dependence. Peaks III, IV and V hydrolysed Z-Ala-Arg-Arg-NNap-OMe rapidly; they also inactivated aldolase and were strongly inhibited by leupeptin. They are probably isoenzymes of cathepsin B1. Peak I showed these properties to a relatively small extent. 7-(N-Benzoyl-DL-argininamide)-4-methylcoumarin appears to be an alternative substrate for cathepsin B1; it was hydrolysed also by peak I, but relatively less rapidly. Peaks I and II were inhibited more than peaks III, IV and V by a muscle extract. Total activity of the Bz-Arg-NH2-hydrolysing enzyme in extensor digitorum longus muscle increased after denervation.

Animals↗
PubMed1979

Carrier detection in Duchenne muscular dystrophy: Assessment of the effect of age on detection-rate with serum-creatine-kinase-activity.

In 40 known carriers of the gene for Duchenne muscular dystrophy (mean age 38 years) the detection-rate with a standard assay of serum-creatine-kinase was 53%. In 52 daughters of known carriers (mean age 16 years) the detection-rate was 45% after correction of age. This implies a much higher detection-rate (about 90%) in young carriers and suggests that discrimination between carriers and noncarriers may best be achieved by testing in childhood.

Adolescent↗
PubMed1979

An evaluation of some carrier detection techniques in Duchenne muscular dystrophy.

Some recently described abnormalities in the serum and red cell membranes in Duchenne dystrophy have been examined as methods of carrier detection in a single-blind controlled study. Twelve carriers (4 definite, 3 probable and 5 possible carriers previously found to have raised creatine kinase levels) and 12 normal female controls of the same age, were examined on 3 separate occasions at approximately two-weekly intervals. Analysis of age-dependent red cell shape changes, serum haemopexin levels, red cell K+ efflux rate, sensitivity of red cell ghost membrane ATPase to ouabain, membrane protein phosphorylation studies and lactate dehydrogenase isoenzyme profiles on agarose gel electrohoresis all failed to distinquish carriers from controls. The carriers suffered muscle cramps more frequently than the controls and all but one carrier and two control subjects were correctly identified by manual muscle strength testing, certain proximal muscles in paricular being consistently weaker in carriers than in the control group subjects. Scalar electrocardiography revealed higher values for the R/S ratio in Leads V1 and V2 and the sum (R-S) in V2.

Adenosine Triphosphatases↗
PubMed1978

Removal of extracellular fluid from muscle: assessment of a method.

Controlled compression of mouse biceps brachii muscle caused only partial extrusion of an extracellular protein (125I-albumin) from the muscle. Concentrations of sodium and potassium in the expressed fluid at any stage of compression did not correspond with concentrations expected for extracellular fluid. This procedure, therefore, does not selectively remove extracellular fluid from muscle.

Albumins↗
PubMed1977

Effect of ouabain upon erythrocyte membrane adenosine triphosphatase in Duchenne muscular dystrophy.

The adenosine triphosphatase activity of erythrocyte ghosts from patients with Duchenne muscular dystrophy was inhibited by 10(-4) M ouabain to a smaller extent than in normals, when measured in the presence of either high or low concentrations of sodium or potassium ions. The inhibition by ouabain of the enzyme in normal ghosts, measured with low sodium or potassium ions, was less if the erythrocytes were first incubated with plasma from Duchenne patients than if incubated with normal plasma. Similar results were obtained when the ghosts themselves were incubated with Duchenne or normal plasma before assay.

Adenosine Triphosphatases↗
PubMed1977

The effect of cortisone on protein breakdown and synthesis in rat skeletal muscle.

The effect of cortisone administration on the rates of muscle protein breakdown and synthesis has been studied in the rat extensor digitorum longus muscle. Cortisone acetate (100 mg/kg body weight/day) was administered intraperitoneally for 1--3 days. Muscle wieght and protein content were significantly reduced by cortisone administration. Rates of protein breakdown were measured by tyrosine release from the isolated muscle into the intracellular pool and medium during a 2-h incubation with cycloheximide to block protein synthesis. Rates of protein synthesis were assayed by [14C]tyrosine incorporation into protein of the isolated muscle during a 2-h incubation. Cortisone administration inhibited significantly the rate of protein synthesis after 1--3 days treatment and also reduced significantly the rate of protein breakdown per muscle after 3 days treatment. The synthesis of myofibrillar and soluble proteins was affected to the same extent. These results strongly suggest that the effect of cortisone administration on muscle protein is mainly through its inhibition of protein synthesis rather than through an acceleration of protein breakdown.

Animals↗
PubMed1976

Separation of rat muscle aminopeptidases.

By means of chromatography on DEAE-Sephadex, two arylamidases (hydrolysing L-arginine 2-naphthylamide) and three dipeptidyl peptidases (hydrolysing dipeptide 2-naphthylamides) were distinguished in extracts of rat muscle. However, the arylamidase from the larger peak also hydrolysed the dipeptide 2-naphthylamides. Glycyl-L-arginine amide, an alternative substrate for dipeptidyl peptidase I, was not hydrolysed by arylamidase. L-Leucine amide was hydrolysed by an enzyme, presumed to be leucine aminopeptidase, from a separate peak, but was also hydrolysed by arylamidase. Arylamidase, dipeptidyl peptidase III and most of the leucine aminopeptidase could be extracted from the muscle with a neutral salt solution, but dipeptidyl peptidase I was extracted only in the presence of Triton X-100; dipeptidyl peptidase II showed an intermediate extraction behaviour.

Aminopeptidases↗