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Biomedical subjects

M Murai

Publications and source records attributed to M Murai.

At least 343 records · Page 19Linked to original sources
PubMed1976

Use of plasma protein fraction in preservation of cadaveric kidneys.

We have compared 23 cadaver kidneys preserved with cryoprecipitated plasma (CPP) with 23 consecutive cadaver kidneys preserved with plasma protein fractions (PPF). In both groups the MOX-100 Waters machine was used. The PPF solution does not contain any fibrinogen or gamma globulin. The harvesting characteristics of both groups were comparable. Pulsatile perfusion time in the PPF group was up to 46 hours and in the CPP group was up to 44 hours. In the PPF group, 20 kidneys achieved immediate function upon transplant (85 percent). Two underwent periods of acute tubular necrosis (ATN) and one kidney never worked. In the CPP group, 18 kidneys achieved immediate function (78 percent). Two underwent periods of ATN and three never achieved satisfactory function. From this clinical experience, PPF is as effective as CPP for the preservation of kidneys up to 44 hours prior to transplant. The advantages of the PPF are easy availability, long shelf life, simple preparation, low cost, freedom from risk of hepatitis, and theoretical absence of antibody against the kidney. Graft and patient survival at 6 months showed no statistical difference.

Adolescent↗
PubMed1975

Effect of sodium dodecyl fulfate on the dissociation of bovine liver catalase.

Native bovine liver catalase [EC 1.11.1.6] and catalase acetylated with N-acetylimidazole (AI) both combined with sodium dodecyl sulfate (SDS) to form catalase-SDS complexes. The differences between native and acetylated catalase bound to SDS were investigated as regards enzymatic activity, absorption spectra, ORD and CD, sedimentation velocity and fluorescence spectra. It was found that the binding of SDS with both catalases depended on incubation time and SDS concentration, and that the acetylation of catalase had some protective effect on the denaturation of the molecule by SDS, which may be ascribed to a reduction of ionic interaction between SDS and the protein on acetylation. The native catalase was found to split into three smaller components on incubation with 1% SDS for 96 hr, whereas the acetylated catalase split into two smaller components. These smaller components were isolated by gel filtration through Sephadex G-100. The isolated components has estimated molecular weights of 60,000, 30,000, aide. It seemed likely that the modification occurred stepwise. Approximately 26% of the carboxyl groups of fibrinogen was modified finally. The modified fibrinogen had no interaction with cationic detergent, and did not form any complex with the detergent. In dilute acid, fibrinogen was observed to show only a slight interaction with cationic detergent. It is probable that the exposed and ionized carboxyl groups are essential for the formation of a complex between fibrinogen and cationic detergent.

Acetylation↗