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Biomedical subjects

A Yoshida

Publications and source records attributed to A Yoshida.

At least 1,297 records · Page 72Linked to original sources
PubMed1974

Material isolated from normal and variant human liver that immunologically crossreacts with alpha1-antitrypsin.

A material that strongly reacts with antibodies against alpha(1)-antitrypsin, but has little trypsin inhibitory capacity, has been isolated and purified to homogeneity from human liver. The molecular weight of the crossreacting material is about 18,000, which is significantly lower than that of serum alpha(1)-antitrypsin. The material isolated from the liver of a homozygous variant subject (ZZ) with alpha(1)-antitrypsin deficiency is readily distinguished by electrophoresis from the material extracted from a normal (MM) subject. The tissues from a heterozygous variant subject (MZ) contain the two components. The immunologically crossreacting material is presumably synthesized by the gene that codes for alpha(1)-antitrypsin.

Animals↗
PubMed1973

Hemolytic anemia and G6PD deficiency.

The severity of enzyme deficiency often does not correlate well with the clinical severity of genetic diseases. Thus, some G6PD variants associated with severe enzyme deficiency, such as Union and Markham, cause no hemolytic problem, while some variants associated with less severe deficiency, such as Manchester, Alhambra, and Tripler, cause chronic hemolytic anemia. The kinetic characteristics of these variant enzymes have not explained the discrepancy. However, examination of the normal and variant enzymes under simulated physiologic conditions, with the effects of various intermediate metabolites and co-enzymes in red cells being taken into consideration, reveal that the G6PD's from hemolytic variant subjects are strongly inhibited by a physiologic concentration of NADPH because of their high Michaelis constant for NADP or low inhibition constant for NADPH, and they are more sensitive to inhibition by ATP. These variant enzymes cannot generate enough NADPH in red cells to maintain an adequate concentration of reduced glutathione. The nonhemolytic variant enzymes are far less sensitive to the inhibition by NADPH because of their low Michaelis constant for NADP and high inhibition constant for NADPH. The physiologic activity of these nonhemolytic variant enzymes is estimated to be more than 30 percent of the activity of the normal G6PD, and this activity is adequate to maintain the red cells unhemolyzed.

Adenosine Triphosphate↗
PubMed1973

G6PD Toronto.

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Adult↗