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Biomedical subjects

M Kaminski

Publications and source records attributed to M Kaminski.

At least 181 records · Page 10Linked to original sources
PubMed1978

Heterosis in the codominance model: electrophoretic studies of proteins in the chicken-quail hybrid.

1. Electrophoretical comparisons was carried out on qualitative and quantitative differences of three proteins in the cock-quail hybrid: albumin, immunoglobulin and hemoglobin. All three components correspond to situations of codominance. 2. Heterosis was demonstrated twice: the immunological potentialities of the hybrid are increased by its possession of two types of Ig G; the affinity of hemoglobin for oxygen can be better regulated in the hybrid than in both parental species. 3. Proportions of the codominant parental components in the hybrid are different in the case of the three investigated proteins; this fact probably reflects the relative importance of the quantitative regulation of gene products in the hybrid.

Animals↗
PubMed1978

Common and species-specific esterases of Equidae--IV. Horse of przewalski, onager and Zebra hartmannae.

1. Among several species of Equidae only E. przewalskii possesses a serum esterase identical with that of E. caballus. 2. The esterases of Hemionidae differ slightly from that of domestic horse by electrophoretic migration and by antigenic structure. 3. Zebras (grevyi, burchelli) appear devoid of this component but Z. hartmannae possesses an esterase of high enzymatic activity, differing notably from that of horse by electrophoretic and antigenic properties.

Animals↗
PubMed1978

The null allele in the horse esterase (Es) system detected by enzyme assay and rocket immunoelectrophoresis in heterozygous animals.

The detection of the recessive null allele of horse serum esterase (Es) is possible in heterozygotes Es+/EsO which by starch gel electrophoresis appear like homozygotes Es+/Es+. Two methods are proposed, the titration of enzymatic activity of esterase and the immunochemical titration of esterase as antigen. These methods can be applied to solve the cases of suspect parentage or in population studies.

Alleles↗
PubMed1978

Alcohol consumption in pregnant women and the outcome of pregnancy.

A prospective study of more than 9000 women shows that during pregnancy, women consuming alcoholic beverages in excess of 40 cl of wine per day have an increased risk of the following unfavorable pregnancy outcomes: (1) the risk of stillbirth is elevated, especially for death from abruptio placentae: (2) mean birth weight is lower, and the risk of a small-for-date infant is increased; (3) placental weight is also decreased. Although heavier drinkers differ from lighter drinkers in a certain number of variables that are risk factors for the outcome of pregnancy, the increase in risk with increased alcohol consumption remains evident after adjustment for these confounding variables. The increase in risk for heavier drinkers appears to be due to beer consumption, in spite of the lower average amount of ethanol consumed by beer drinkers as compared to wine drinkers.

Adult↗
PubMed1978

[Outcome of pregnancy and prenatal care among immigrant women (author's transl)].

A retrospective survey on a representative sample of births in France in 1972 relating to more than 11000 women showed the amount of perinatal pathology among immigrants as compared with French women: a higher rate of foetal or neonatal distress, a three to four times higher stillbirth rate among Portuguese and North African women, a prematurity rate more than twice as higher among North African women. When differences in parity and socio-cultural level between immigrant and French women were allowed for, there remained a higher rate of perinatal pathology among immigrants. Prenatal care was also more often inadequate among immigrants, even when taking into account their low socio-cultural standard. Attitude towards prenatal care was highly influenced by the level of adaptation in France. But, even with equal prenatal care, perinatal pathology was higher among immigrant women: being an immigrant is a risk factor in itself.

Acculturation↗
PubMed1976

[Biochemical polymorphism in the red partridge (Alectoris rufa)].

Egg white proteins, hemoglobin, serum proteins and enzymes from Alectoris rufa have been examined by starch gel electrophoresis. All three genetic parameters, mean proportion of loci polymorphic per population (P), mean numbers of alleles per locus (A), and mean proportion of loci heterozygous per individual (H) are given for Alectoris rufa, and comparison were made between the proteins of the related species Coturnix coturnix japonica.

Alkaline Phosphatase↗
PubMed1975

[Biochemical polymorphism of Japanese quail (Coturnix coturnix japonica): comparison of functionally different proteins (author's transl)].

The polymorphism observed among the enzymes involved in the respiratory metabolism (lactate dehydrogenase, malate dehydrogenase, phosphoglucomutase, phosphohexoseisomerase, glucose-6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase fructose 1-6 diphosphate dehydrogenase) is less important than that of the enzymes physiologically less essential, such as the various esterases, the alkaline phosphatase, the alcohol dehydrogenase, and of the non-enzymatic proteins (ovalbumin, ovoglobulins, ovomucoid, conalbumin, transferrin, etc.).

Alcohol Oxidoreductases↗
PubMed1975

Multiple forms of tryptophanyl-tRNA synthetase from beef pancreas.

Three different forms of tryptophanyl-tRNA synthetase can be isolated from pancreatic extracts. Structural, immunological and catalytic properties of these various forms have been compared. The native enzyme is a dimeric molecule of molecular weight 108000. Two other forms, of molecular weight 85000 and 82000, are composed of two polypeptide chains identical with the carboxyl terminal region of the native subunits. These molecules are supposed to derive from the original protein by removal, from the amino-terminal part of each subunit, of a fragment of 11000 to 13000 molecular weight. Such removal modifies the shape and the stability of the molecule and decreases its specific acitvity. The origin of the derived forms is attributed to proteolysis. In fact, limited proteolysis of purified tryptophanyl-tRNA synthetase, in its native form, by elastase, results in the formation of an active compound, similar to one of the tryptophanyl-tRNA synthetase derived forms. Furthermore, incubation with "elastolytic fractions" prepared from pancreatic extracts presenting a particularly high level of proteolytic activity produces the same cleavage in tryptophanyl-tRNA synthetase polypeptide chain.

Amino Acids↗