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Biomedical subjects

G Murano

Publications and source records attributed to G Murano.

At least 55 records · Page 3Linked to original sources
PubMed1982

Rabbit fibrin: characterization of the separated chains.

In preparation for studies of the time course of production in vivo of the constituent chains of rabbit fibrin, we characterized the structural features of the fibrin molecule. Fibrin was isolated from plasma and reduced and alkylated. The alpha, beta, and gamma chains were separated by CM-cellulose chromatography and their molecular weights and amino acid compositions were determined. The gamma chain was sequenced 36 steps with 32 positive identifications and the beta chain, 12 steps with 12 identifications. No major differences between the sequences of these chains and those of man, chicken, and dog were noted.

Amino Acid Sequence↗
PubMed1981

International collaborative study on the assay of commerically available high and low molecular weight urokinases.

Urokinases of different molecular weights are now commerically available. An international collaborative study (eight laboratories) has been conducted to investigate the effect of type and concentration of plasminogen on the assay of two different urokinase preparations against the International Reference Preparation (IRP). Considerable inter-laboratory variation in relative potency estimation was found, and a small effect of plasminogen concentration, independent of type, was apparent.

Biological Products↗
PubMed1981

Human antithrombin III heterogeneity.

Crossed immunoelectrophoretic patterns were obtained on three patients with a congenital deficiency of anti-thrombin III (AT-III), and on normal single donor and "pooled" plasma controls. In the presence of heparin (incorporated into the agarose gel matrix), the AT-III of normal human plasma was separated into four components: two major, faster-moving components, and two minor, slower-moving components. The three patients with congenital deficiency of AT-III (levels approximately 50% of normal) appeared to possess only one of the faster-moving components, and one of the slower-moving components.

Antithrombin III↗
PubMed1980

The inhibition of high and low molecular weight urokinase in plasma.

The rates of inhibition of high molecular weight (HMW) and low molecular weight (LMW) urokinase (UK) incubated in plasma or with purified antithrombin III (AT-III) were compared. Using a fibrinolytic assay system to determine residual biologic activity, polyacrylamide gel electrophoresis to demonstrate the formation of complexes, and selective immunoprecipitation techniques to identify the plasma inhibitors participating in the neutralization process, it was established that: (A) HMW-UK is inhibited more rapidly than LMW-UK, both in plasma and with purified AT-III; (B) heparin (3--10 U/ml accelerates the neutralization process in both systems, but only slightly; and (C) in plasma, several inhibitors, alpha 2-macroglobulin, alpha 1-antitrypsin, and antithrombin III, neutralize the activity of HMW-UK and LMW-UK.

Animals↗
PubMed1978

The "Hageman" connection: interrelationships of blood coagulation, fibrino(geno)lysis, kinin generation, and complement activation.

The activation pathways for the generation of enzymes involved in blood clotting, clot lysis, complement activation, and kinin generation are briefly reviewed. The interrelationship of the four systems is illustrated by the multiple functions of four key enzymes: Factor XIIa, kallikrein, plasmin, and C1 esterase. The pivotal role of Factor XIIa in establishing this connection is elucidated.

Blood Coagulation↗
PubMed1978

Lack of inhibition of hog renin by heparin.

These experiments were performed to test if heparin inhibits the production of angiotensin I from rat renin substrate acted upon by either rat or hog renin. Substrate was prepared from the plasma of nephrectomized rats; commercially prepared hog renin and heparin (0-50 units/ml, final concentration) were added and angiotensin I production was measured by radioimmunoassay following incubation of the mixture at 37-38 degrees C for 30 min. Heparin had no effect on the radioimmunoassay for angiotensin I, nor on the Vmax nor the Km of the renin-renin substrate reaction. Heparin (0 and 50 units/ml, final concentration) was added to rat plasma which contained renin and renin substrate. No effect of heparin on the rate of production of angiotensin I was observed in this system. In conclusion, rat and hog renin are not inhibited by heparin within the range of concentrations used.

Angiotensin I↗
PubMed1977

[Prof. Ivo Nasso].

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History, 20th Century↗