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Biomedical subjects

M Kondo

Publications and source records attributed to M Kondo.

At least 1,405 records · Page 78Linked to original sources
PubMed1979

Effect of a streptococcal preparation on the complement system.

Streptococcal preparation OK-432 (Picibanil), clinically being used as an immunopotentiator, has been shown to activate the complement system either through the classical or the alternative pathway in vitro [15]. In this experiment, OK-432 was found to increase serum complement level in guinea pigs, and in human without malignancy, when investigated by hemolytic assay using sensitized sheep erythrocytes (EA) for the classical pathway activity and unsensitized rabbit erythrocytes (RaE) for the alternative pathway activity. Assay of complement components revealed a significant increase in C3, but decrease in Clq, while no specific tendency was observed in C4, C5, C9, properdin, C3 activator and Cl-inhibitor. These evidences suggested that OK-432 might potentiate immune response of the host by elevating serum complement level, in addition to activate the complement system.

Aged↗
PubMed1978

Oxygen-binding characteristics of three extracellular haemoglobins of Artemia salina.

The oxygen-binding characteristics of the three extracellular haemoglobins of brine shrimp (Artemia salina) were studied in vitro by using highly purified preparations. Haemoglobin I is induced last in the development of brine shrimps when functional gills are formed. It has the lowest oxygen affinity (p(50) 5.34mmHg), an intermediate Bohr effect (ø -0.09 at 20 degrees C) above pH8 and a temperature-sensitivity (DeltaH -44.8 to -45.6kJ/mol at pH8-9) comparable with those observed with other invertebrate haemoglobins [Weber & Heidemann (1977) Comp. Biochem. Physiol. A57, 151-155]. Haemoglobin II, which is the first to be induced, soon after hatching of nauplius larvae, persists generally throughout the whole adult life. It has an intermediate oxygen affinity (p(50) 3.7mmHg), the highest Bohr effect (ø -0.21 at 20 degrees C) above pH8 and a similar temperature-sensitivity (DeltaH -46.0 to -54.8kJ/mol at pH8-9) as haemoglobin I. However, haemoglobin III, which is induced second several hours after the induction of haemoglobin II but disappearing from the haemolymph in the middle of adult life, has the highest oxygen affinity (p(50) 1.8mmHg), the lowest Bohr effect (ø -0.03 at 20 degrees C) above pH8.5 and a high resistance against temperature variation between 10 and 25 degrees C at pH8.5-9 (DeltaH -22.6 to -23.0kJ/mol). At pH7.5-8, haemoglobin III exhibits a similar temperature-sensitivity under 30 degrees C as do other haemoglobins. All three haemoglobins have a rather low co-operativity, with Hill coefficients (h 1.6-1.9 at pH8.5), which are dependent on both pH and temperature. The highest co-operativity was observed at 20 degrees C and pH9 for haemoglobins I and II, whereas it was at 27 degrees C and pH8.5 for haemoglobin III. Thus the oxygen-binding behaviour of haemoglobin III in vitro is significantly different from those of haemoglobins I and II and indicates possibly its specific physiological role in vivo in the adaptive process in the natural environment.

Animals↗
PubMed1978

Evidence for a dimeric form of Artemia salina extracellular hemoglobins with high-molecular-weight subunits.

The brine shrimp, Artemia salina, produces at least three chemically and ontogenetically distinct extracellular hemoglobins (Hb-I, Hb-II and Hb-III). The estimated molecular weights of these hemoglobins are 240000-260000, containing 14 heme groups based on the iron and heme contents of a molar species. Hb-II, which corresponds to a minimal molecular weight of about 18 000 per heme [Moens, L. and Kondo, M. (1977) Biochem. J. 165, 111-119]. Denaturation of the reduced and alkylated hemoglobins with 8 M guanidine hydrochloride revealed apparently one polypeptide chain having a molecular weight of 126 000. Thus a single native hemoglobin molecule should be composed of two of these high-molecular-weight subunits each of which is bound with seven hemes. Upon sodium dodecyl sulfate/polyacryamide gel electrophoresis of either native hemoglobins or isolated subunits it was found that the 126 000-Mr polypeptide was cleaved specifically into two unequally-sized fragments of Mr 50 000 and 80 000. Further denaturation of native hemoglobins with urea at pH 2.5 or 11 followed by sodium dodecyl sulfate gel electrophoresis confirmed these results. The amino acid compositions determined for native Hb-II and its subunit and fragments are found to be very similar, implying that no specifically localized amino acid sequences are present and that the subunit globin chain could be composed of seven similar repeat units (Mr approximately 18 000) being linked covalently to one another. The amino acid compositions of Hb-I and Hb-III showed only minor differences to that of Hb-II.

Amino Acids↗
PubMed1978

A case of Menetrier's disease associated with protein-losing gastropathy and abnormal serum complement profile.

A 44-year-old man with Menetrier's disease associated with protein-losing gastropathy and with abnormal serum complement profile is reported. He was treated by an antifibrinolytic compound tranexamic acid (trans-AMCHA) since he was found to have elevated fibrinolytic activity in the biopsied gastric mucosa. The therapy brought his serum protein from 3.8 g/dl to 5.6g/dl, however could not reduce his mucosal disorder. Substitution of a placebo for trans-AMCHA resulted in marked depression of his serum protein to 3.7 g/dl. It was concluded that trans-AMCHA was effective in raising his serum protein to a certain extent but failed to block the vicious circle of "mucosal disorder", "increased tissue fibrinolysis" and "hypoproteinemia" (Kondo, M. et al. Gastroenterology 70, 1045, 1976). Abnormal serum complement profile seen in this patient was found to be due to cold activation of the classical complement pathway (Kondo, M. et al. J. Immunol. 117, 486, 1976). Although no correlation between the phenomenon and Menetrier's disease has been clarified yet, the appearance of wheezing as in asthma when exposed to cold suggested that cold activation of complement occurred in vivo and resulted in increasing of the vascular permeability in the lungs.

Adult↗