Biomedical subjects

M Tozuka

Publications and source records attributed to M Tozuka.

At least 55 records · Page 3Linked to original sources

PubMed1990

[Analysis of cross-linked fibrin and fibrinogen degradation products with SDS-PAGE and immunoblot].

SDS-PAGE and immunoblot technique with anti-FDP-D, -FDP-E, -fibrinogen antibody or anti-FDP-DD monoclonal antibody were applied to analyze FDP fragments prepared from cross-linked fibrin and fibrinogen with plasmic digestion in vitro. FDP fragments of DY(260K), DD(187K), X(245K), Y(166K), D(77K, 97K), E1(58K), E2(46K) and E3(40K) were identified from data of molecular weight and reactivity to four antibodies referred to reports of other investigators. Serum FDP fragments from five DIC suspected patients were analyzed by the same methods. In two patients' sera, DD fragment was a main component, and in the other three patients' sera, D fragment was a main fraction. Proportions of high molecular weight fragments of FDP were considerably different in patients' sera. Appearance of D fragment in our cases was considered to be derived from unstable fibrin (fibrin monomer and dimer) rather than from fibrinogen. Molecular weight of DD fragments from patients' sera had heterogeneity (160 approximately 180K), and the values were different from that (187K) prepared from cross-linked fibrin. In conclusion, SDS-PAGE and immunoblot analysis of serum fragments of FDP will be an useful technique to investigate the clinical and pathological condition of DIC.

Disseminated Intravascular Coagulation↗

PubMed1989

Purification and characterization of two high-density-lipoprotein-binding proteins from rat and human liver.

The liver plays a major role in the metabolism of plasma high-density lipoprotein (HDL). Several groups have postulated, but others refuted, the existence of a classical membrane receptor which recognizes HDL. In the present study, we identified and purified two liver HDL-binding proteins of 120 kDa (HB1) and 100 kDa (HB2), with apparent specificity for HDL3 devoid of E apolipoprotein. The plasma membrane was the richest source of the HDL-binding protein. Both proteins bound A-I and A-II apolipoproteins and retained HDL-binding activity after final purification. HB1 activity, but not that of HB2, was lost after treatment with beta-mercaptoethanol, but reduction did not change the apparent molecular mass of either protein. Antibodies against HB1 or HB2 did not cross-react, and preliminary structural investigations provide evidence to suggest that HB1 and HB2 are not structurally related. We thus provide evidence for at least two liver plasma-membrane proteins which bind HDL apolipoproteins, suggesting that protein-protein interaction participates to some degree in the mechanism of HDL recognition by cells.

Animals↗

PubMed1989

Monoclonal antibodies to human A-I apolipoprotein and characterisation of cyanogen bromide fragments of apoA-I.

Several monoclonal antibodies to human A-I apolipoprotein were produced after immunising mice with pure delipidated apoA-I. These monoclonal antibodies were characterised for their ability to react with whole lipoproteins, apolipoproteins and fragments of apoA-I generated by cleavage with cyanogen bromide. The data suggest that production of monoclonal antibodies using apoA-I as antigen was influenced by two major epitopes subsequently localised to cyanogen bromide fragments 1 and 3, and have been designated antibodies 1----5 A-IB and 6----10 A-IB, respectively. Cyanogen bromide fragments were first purified to homogeneity before screening by competitive displacement or immunoblotting procedures. Definitive characterisation of one antibody series (1----5 A-IB) depended ultimately on Western blotting following isoelectric focusing of purified apoA-I fragments. This technique identified the epitope for these antibodies to fragment 1, an identification not fully concluded from competitive displacement studies. These studies have also revealed the presence of microheterogeneity in fragment 1 (as well as in fragment 4) of apoA-I, suggesting that structural variations in several regions may account for the polymorphism observed in this apolipoprotein.

Animals↗

PubMed1983