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A Stratil

Publications and source records attributed to A Stratil.

At least 73 records · Page 4Linked to original sources
PubMed1988

Further studies of the plasma alpha 1 B-glycoprotein polymorphism: two new alleles and allele frequencies in Caucasians and in American blacks.

Two new alleles (A1 B*3 and A1 B*4) of human plasma alpha 1 B-glycoprotein (alpha 1 B) were reported. alpha 1 B phenotyping was done by using either a simple method of two-dimensional (2-D) agarose gel-horizontal polyacrylamide gel electrophoresis (PAGE) followed by protein staining or by one-dimensional horizontal PAGE and immunoblotting. Seven different alpha 1 B phenotypes (1-1, 1-2, 1-3, 1-4, 2-2, 2-3 and 3-3) were observed; phenotypes 1-3 and 1-4 were differentiated from each other only by the 2-D method. The respective frequencies Af A1 B*1, A1 B*2, A1 B*3 and A1 B*4 alleles in the studied populations were estimated as follows: American Blacks (New York) 0.732, 0.204, 0.064, 0; American Whites (New York) 0.947, 0.053; Czechs (Mĕlník) 0.964, 0.034, 0, 0.002; Slovaks (Bratislava and Trencin) 0.977, 0.023, 0, 0. The population of American Blacks showed a much higher degree of alpha 1 B polymorphism (polymorphism information content = 0.37) than the Caucasian populations that have been studied.

Alleles↗
PubMed1987

Genetic polymorphism of human plasma alpha 1B-glycoprotein: phenotyping by immunoblotting or by a simple method of 2-D electrophoresis.

Genetic polymorphism of human plasma (serum) alpha 1B-glycoprotein (alpha 1B) was observed using one-dimensional horizontal polyacrylamide gel electrophoresis (PAGE) pH 9.0 of plasma samples followed by Western blotting with specific antiserum to alpha 1B. A simple method of two-dimensional agarose gel electrophoresis (pH 5.4)-horizontal PAGE (pH 9.0) of plasma samples, followed by general protein staining, was reported as an alternative method for alpha 1B typing. The three different phenotypes of alpha 1B observed (designated 1-1, 1-2, and 2-2) were apparently identical to those reported by Altland et al. (1983), who used double one-dimensional electrophoresis. Family data supported the hypothesis that the three alpha 1B phenotypes are determined by two codominant alleles at an autosomal locus, designated A1B. Allele frequencies in a Swedish population were: A1B1, 0.937; A1B2, 0.063; PIC, 0.111. For clues on linkage relationships of human A1B, the previously known linkages of A1B in pigs and horses, including the one between A1B and the gene that determines susceptibility to malignant hyperthermia in pigs were discussed.

Blood Proteins↗
PubMed1987

Sheep haemopexin: immunological cross-reactivity with other vertebrate sera and evidence for the absence of haemopexin in some mouflon.

A monospecific antiserum to sheep haemopexin was produced in rabbits. By using this antiserum, as well as absorbed antisera to sheep and mouflon serum proteins, it was proved that some mouflon sera lack haemopexin. In immunodiffusion, when using the monospecific antiserum, immunoprecipitates were present only in species' belonging to suborder Ruminantia. None of the other mammalian, nor any of the avian, reptilian, amphibian and fish species tested, showed reaction.

Animals↗
PubMed1987

Pig plasma postalbumin-2 (alpha 1B-glycoprotein): isolation, partial characterization and immunological cross-reactivity with other mammalian sera.

1. Components of pig plasma postalbumin-2 (PO2) protein, after rivanol-ammonium sulphate fractionation of plasma, were separated from other proteins by an easy and rapid method of horizontal double-one dimensional IPG-PAGE. The protein was recovered from polyacrylamide gel by combination of electrophoresis and isoelectric focusing. 2. The mol. wt of PO2 was estimated to be 68,000, using SDS-PAGE. 3. Amino acid and carbohydrate compositions of PO2 were very similar to those of human plasma alpha 1B-glycoprotein (alpha 1B), confirming that PO2 is the porcine homologue of human alpha 1B. 4. Neuraminidase treatment resulted in a decrease of electrophoretic migration velocity of all four studied components of PO2. 5. Homologous proteins to pig PO2 (alpha 1B) were observed, not only in human plasma but also in plasma of dog, horse and rabbit, by immunoblotting.

Amino Acids↗
PubMed1987

Polymorphic plasma postalbumins of some domestic animals (pig PO2, horse Xk and dog Pa proteins) identified as homologous to human plasma alpha 1B-glycoprotein.

Pig, horse and dog plasma proteins, separated by horizontal polyacrylamide gel electrophoresis (pH 9.0) and electrophoretically transferred to nitrocellulose membranes, were tested for cross-reaction with antiserum to human plasma alpha 1B-glycoprotein (alpha 1B). The results showed that one previously reported polymorphic plasma postalbumin in each of these species (pig PO2, horse Xk and dog Pa protein) was homologous to human plasma alpha 1B. In the light of the previously known genetic linkages in these species, this implied: (1) alpha 1B gene is close linked to Phi, Pgd and Hal (halothane sensitivity locus) loci in pigs; and (2) alpha 1B gene is linked to ME1 and Phi loci in horses. This suggested that the alpha 1B gene may also be found to be closely linked to gene(s) controlling susceptibility to malignant hyperthermia in humans and other mammals.

Alpha-Globulins↗
PubMed1985

Partial characterization of transferrins of catfish (Silurus glanis L.) and pike (Esox lucius L.).

Basic composition and properties of isolated transferrins of Silurus glanis and Esox lucius have been compared. In transferrin of S. glanis carbohydrate is absent, but it is present in transferrin of E. lucius (2.5%). The N-terminal amino acid is alanine in both species. Mol. wts are 68,400 (S. glanis) and 86,800 (E. lucius). Transferrins of the two species are heterogeneous, but genetic polymorphism was not observed.

Amino Acids↗
PubMed1985

Phylogenetically more conservative epitopes among monoclonal antibody-defined antigenic sites of human transferrin are involved in receptor binding.

Of eight monoclonal antibodies raised against human transferrin, one (H.TF-14) cross reacted with pig and rabbit transferrins and one (H.TF-1) showed cross-reactivity with horse and dog transferrins. While rabbit and pig transferrins exhibited the same patterns of binding to MOLT-3 cell receptors as human and horse transferrins, binding of mouse and dog transferrins was weaker and bovine and carp transferrins gave entirely negative results. The results of these competitive binding experiments were confirmed by a biological test in which bovine transferrin had no effect on the growth of MOLT-3 cells when added to a serum-free medium. The observed correlation between cross-reactivity of anti-transferrin monoclonal antibodies and the binding abilities of transferrins to the MOLT-3 cell receptors may be associated with the conservatism of the part of the transferrin molecule recognized by the cell receptor.

Animals↗
PubMed1984

A study of a polymorphic globulin in the serum of Silurus glanis L.

A polymorphism of S-globulin was detected in serum of Silurus glanis L. by starch gel electrophoresis. Three phenotypes were observed which are apparently controlled by two codominant alleles, SgA and SgB, of an autosomal locus, Sg. Although on electrophoresis S-globulin and transferrin have similar mobilities, the properties of the two proteins differ.

Alleles↗
PubMed1984

Heterogeneity of horse transferrin: the role of carbohydrate moiety.

Homozygous horse transferrin (Tf O) is highly heterogeneous. In starch gel electrophoresis it gives at least 9 zones. Two main components (2a and 4b) were purified by rivanol and ammonium sulphate precipitation, DEAE-Sephadex chromatography and SP-Sephadex chromatography. Molecular weights of 75 200 and 80 500 for components 2a and 4b, respectively, were determined by sedimentation equilibrium ultracentrifugation. Amino acid compositions of the two components were similar, and there were no differences in the N-terminus (glutamic acid followed by glutamine) and the C-terminus (valine). Differences were found in carbohydrate composition between components 2a and 4b. Component 2a contained 10 moles of sugar components per mole of protein (4 hexoses, 4 hexosamines and 2 sialic acids), while component 4b contained twice the number of both total carbohydrates and individual sugar components. Carbohydrates were identified as mannose and galactose (ratio mannose: galactose approximately equal to 1.5:1), N-acetylglucosamine and N-acetylneuraminic acid. At present it is not clear whether the difference between the two components resides solely in the difference of carbohydrate contents. It is proposed that component 2a has one diantennary glycan, while component 4b has two.

Amino Acids↗
PubMed1984

Haemopexin in sheep, mouflon and goat: genetic polymorphism, heterogeneity and partial characterization.

Benzidine staining of starch gels after electrophoresis of sera to which haematin was added revealed polymorphism of haemopexin in sheep, mouflon and goat. In sheep three phenotypes were observed, Hpx A, Hpx AB and Hpx B. Pedigree data support the hypothesis of codominant inheritance from a single locus by two alleles, HpxA and HpxB. Neuraminidase treatment of haemopexin preparations showed that Hpx B covered two variants, B1 and B2, thus indicating genetic control by three alleles (HpxA, HpxB1 and HpxB2). In sheep populations the frequency of HpxB is low. In mouflon, in addition to the two variants that are like those of sheep, absence of haemopexin was observed in some animals, by using starch gel electrophoresis as well as immunoelectrophoresis. In goat, three phenotypes were detected, Hpx A, Hpx AB and Hpx B, differing in migration from those of sheep. Haemopexins of the studied species are heterogeneous. Sialic acid is responsible for electrophoretic heterogeneity of sheep haemopexin. Chemical composition (amino acid and carbohydrate), molecular weight (56 060) and N-terminal sequence (Leu-Pro-Pro-) of sheep haemopexin were also determined.

Alleles↗
PubMed1983

Partial characterization of transferrins of some species of the family Cyprinidae.

1. Transferrins of five cyprinid fishes (Tinca tinca, Ctenopharyngodon idella, Chondrostoma nasus. Hypophthalmichthys molitrix and Aristichthys nobilis) were isolated in a pure state using Sephadex G-100, DEAE-Sephadex and SP-Sephadex. 2. All the transferrins are heterogeneous. In H. molitrix and A. nobilis the heterogeneity is caused partly, but not exclusively, by the presence of sialic acid; in the other species it is independent of sialic acid. 3. Molecular weights ranging from 69,900 (T. tinca) to 78,800 (H. molitrix) were obtained by sedimentation equilibrium ultracentrifugation. SDS-polyacrylamide gel electrophoresis with beta-mercaptoethanol indicated that the transferrins are composed of a single polypeptide chain. 4. Amino acid compositions of all species were similar, the greatest similarity being in the transferrins of H. molitrix and A. nobilis. 5. Carbohydrate was not found in transferrins of T. tinca and C. idella, but was present in A. nobilis (2.63%) and H. molitrix (5.01%). 6. Alanine was N-terminal in C. idella. No N-terminal amino acid was found in T. tinca, H. molitrix and A. nobilis.

Amino Acids↗
PubMed1981

Partial characterization of horse transferrin heterogeneity with respect to the atypical type, Tf C.

In starch gel electrophoresis of horse sera each transferrin variant is formed by a strong anodal band and a weaker cathodal band. An 'atypical' Tf C, has two zones of about equal intensity. Family data show that Tf C is genetically controlled by an allele Tf C at the Tf locus. Frequencies of transferrin alleles in various horse breeds are also presented. After isolation and fractionation of individual transferrin variants (Tf O, Tf D, Tf C) on DEAE-Sephadex, additional weak bands were detected. The two main zones of each variant were isolated in a pure state and treated with neuraminidase. In all three variants studied the electrophoretic mobility of the slower band (2a) was decreased in two steps, and the faster band (4b) in four steps. The mobilities of hands derived from the fast zone (4b) were slower than mobilities of corresponding bands derived from the slow zone (2a). These results suggest the presence of two sialic acid residues in the slow zone, and of four residues in the fast zone. Residual heterogeneity was independent of sialic acid.

Alleles↗
PubMed1979

An unusual transferrin variant in sheep.

An unusual variant, Tf Aw, has been found in sheep transferrins. It position in starch gel electrophoresis is identical with the variant Tf A, but the intensity of corresponding bands is substantially lower. Family analyses prove that the variant Aw is genetically controlled and represents either the product of an unusual allele Tf Aw or the interaction between the allele Tf A and a hypothetical modifying locus.

Animals↗
PubMed1978

Further studies on sheep polymorphic erythrocyte diaphorase.

Starch gel electrophoresis of sheep hemolysates revealed anodically faster, polymorphic NADH/NADPH diaphorase (Dia1) and slower NADH diaphorase (Dia2). Frequencies of alleles Dial F and Dial S for six sheep breeds in Czechoslovakia are given and efficacy for parentage control is discussed. A heterogeneity in Dia2 is caused by a prolonged storage of samples.

Alleles↗
PubMed1976

Polymorphism of transferrin in carp (Cyprinus carpio L.): genetic determination, isolation, and partial characterization.

Seven transferrin variants (A,B,C,D,E,F, and G) have been found in carp sera (Cyprinus carpio L.). Genetic analysis involves five variants and agrees with the hypothesis of simple codominant autosomal inheritance at one transferrin (Tf) locus in spite of the fact that the carp is a tetraploid in relation to other species of the same family. Carp populations from three regions were studied which differed in gene frequencies. Individual populations were in Hardy-Weinberg equilibrium. The polymorphism of carp transferrins can be used for the identification of offspring of single parent pairs, stocked in one pond. Transferrins have been isolated and characterized. Homozygous phenotypes comprised four iron-binding components differing in electrophoretic mobility. This heterogeneity is not caused by sialic acid, which is absent. Amino acid composition, content of hexoses (1 mole/mole of protein) and hexosamines (1 mole/mole of protein), molecualr weight (70,000), and the isoelectric point (5.0) have been determined. No N-terminal amino acid could be detected.

Amino Acids↗