Linkage between the loci for serum albumin and vitamin D binding protein (GC) in sheep

Evidence for close genetic linkage between the loci for serum albumin (ALB) and vitamin D binding protein (GC) in sheep is presented. No recombinants were found in 28 informative offspring of a single ram family. The recombination frequency between the two loci was estimated to be in the range of 0 to 10%. No sign of linkage was observed between the ALB-GC complex and transferrin.     

Linkage between the loci for serum albumin and vitamin D binding protein (GC) in the Japanese quail

Vitamin D binding protein ( GC ) and serum protease inhibitor ( PI ) have been added to genetic markers in the Japanese quail. Both loci were controlled by autosomal codominant alleles named GC^A, GC^B and PI^A, PI^B, PI^C, respectively. Close linkage between the loci for serum albumin ( ALB ) and GC protein is reported. Two recombinants were observed in 145 informative offspring of 14 families. The recombination frequency between the loci was estimated as 0.014±0.006. Thus, GC was assigned to linkage group II in the Japanese quail. No signs of linkage were observed among the loci for the ALB-GC complex, PI. serum prealbumin 2 ( PA2 ), phosphoglucose isomerase ( PG1 ), 6-phosphogluconate dehydrogenase ( PGD ) and esterase-D ( ESD ).     

Evolutionary conservation of the linkage between the structural loci for serum albumin and vitamin D binding protein (Gc) in cattle

Evidence is presented for close genetic linkage between the structural loci for serum albumin and the vitamin D binding protein (Gc) in Belgian Blue and White cattle. Five recombinants were observed in a total of 342 informative offspring. The recombination frequency between the two loci was estimated as 1.5% +/- 0.9. The observed distribution of the haplotypes deviated from the expected one in the population, probably due to selection and significant linkage disequilibrium.     

Evolutionary conservation of the linkage between the structural loci for serum albumin and vitamin D binding protein (Gc) in cattle

Summary. Evidence is presented for close genetic linkage between the structural loci for serum albumin and the vitamin D binding protein (Gc) in Belgian Blue and White cattle. Five recombinants were observed in a total of 342 informative offspring. The recombination frequency between the two loci was estimated as 1.5%± 0.9. The observed distribution of the haplotypes deviated from the expected one in the population, probably due to selection and significant linkage disequilibrium.     

Homology between the human vitamin D-binding protein (group specific component), alpha-fetoprotein and serum albumin

41 Amino acid long N-terminal sequences of the three major human vitamin D-binding proteins (group-specific components Gc1F, Gc1S and Gc2) were characterized: they were identical. By computer analyses, the alignment of this N-terminal sequence with several sequences of human serum pre-proalbumin and human pre-alpha-fetoprotein was established.     

Genetic polymorphism of serum vitamin D-binding protein (GC) in sheep and mouflon

One-dimensional polyacrylamide gel electrophoresis (1D PAGE) followed by immunoblotting revealed genetic polymorphism of GC protein in sheep (variants F, S, V) and mouflon (variants F and S, apparently identical to F and S of sheep). The frequency of Gcs allele ranged from 0.84 to 1.0 in the 12 breeds of sheep studied. GcV allele was observed only in Tsigai breed with a frequency of 0.017.     

Prp (proline-rich protein) genes linked to markers Es-12 (esterase-12), Ea-10 (erythrocyte alloantigen), and loci on distal mouse chromosome 6

The closely linked proline-rich protein (Prp) genes, coding for abundant salivary proteins, are located on distal mouse chromosome 6. They are part of a conserved linkage group that is represented on human chromosome 12p. Two other markers, Ea-10 and Es-12, that were previously unassigned to a chromosome are closely linked to Prp genes in the mouse.     

Investigation of the antigen antibody reaction between anti-bovine serum albumin (a-BSA) and bovine serum albumin (BSA) using piezoresistive microcantilever based sensors

A new microsensor application based on piezoresistive microcantilever technology has been used to study the interaction of anti-bovine serum albumin (a-BSA) with bovine serum albumin (BSA). A thin layer of BSA attached to a glass slide was used as the active sensing layer for the detection of a-BSA in solution. This design produced a large, consistent cantilever deflection when exposed to the analyte. In this system, the cantilever deflection is measured as a simple resistance change in the piezoresistive channel within the cantilever. In a second set of experiments, 3:1 BSA:PEO protein/polymer blended substrates were used as the active sensing layer for the detection of a-BSA in an aerosol delivery. A distinct signature for the analyte, separate from the water vapor carrier, is obtained for this system.     

Mechanism of the binding of 2-(4'-hydroxyphenylazo)benzoic acid to bovine serum albumin

The mechanism of the binding of 2-(4'-hydroxyphenylazo)benzoic acid (HABA) to bovine serum albumin was studied by relaxation methods as well as the binding isotherm using gel chromatography. A single relaxation was observed over a wide range of HABA concentration except at the extremes of high concentration where another slow process was observed. The concentration dependence of the reciprocal relaxation time of the fast process decreased monotonically with increase in concentration of HABA at constant polymer concentration. The data were analyzed on the basis of Brown's domain structure model and were found to be consistent with a sequential binding mechanism. The azohydrazon tautomerism of HABA was identified with the intramolecular step of the complex. The activation parameters of the step, determined from the temperature dependence of the relaxation time of the fast process, showed that this step is rate limited by an enthalpy barrier in both forward and backward directions. Comparison of the activation parameters with those of other serum albumin-ligand systems suggests that there is an enthalpy-entropy compensation in the activation process of the intramolecular step with the compensation temperature at about 270 K; the enthalpy-entropy compensation is thought to be related to the hydrophobic nature of the ligand.     

Genetic serum protein markers (PH,GC, PI) in two South Indian caste populations

The results of HP, GC and PI typings on two caste populations (Relli-I: fruit vendors, Relli-II: scavengers) from Andhra Pradesh (South India) are reported and compared with data obtained on other Indian population samples.     

Genetic serum protein markers (HP,TF, GC and PI) in eight Slovakian population samples

1194 individuals from eight different regions of Slovakia have been typed for haptoglobin (HP) types and for transferrin (TF), group specific component (GC) and alpha-1-antitrypsin (PI) subtypes. Whereas the HP allele frequencies do not show a remarkable regional variability within Slovakia, this could be demonstrated concerning the TF, GC and PI allele frequencies. The reason for these distribution heterogeneities seems to be due to the incomplete panmixia of the Slovakian population by which local variations in the distribution of genetic markers could be maintained.     

Spectroscopic analysis of the binding interaction between tinidazole and bovine serum albumin (BSA)

The interaction between bovine serum albumin (BSA) and tinidazole (Tindamax; 1) in aqueous solution was investigated in detail by means of UV/VIS and fluorescence spectroscopy, as well as through resonance light-scattering (RLS) spectroscopy. The apparent binding constant and number of binding sites were determined at three different temperatures, as well as the average binding distances between 1 and the nearest amino acid residue(s) of BSA, as analyzed by means of F?rster's theory of non-radiation energy transfer. Compound 1 was found to quench the inner fluorescence of BSA by forming a tight 1:1 aggregate, based on both static quenching and non-radiation energy transfer. The entropy change upon complexation was positive, and the enthalpy change was negative, indicating that the observed spontaneous binding is mainly driven by electrostatic interactions.     

Genetic serum protein markers (HP,GC, TF,PI) in four Turkish population samples

Four population samples from different regions of Turkey (Thracia, Karadeniz Bölgesi, West Anatolia and East Anatolia) with a total of 338 individuals have been typed for haptoglobin (HP) and for group specific component (GC), transferrin (TF) and alpha₁-antitrypsin (PI) subtype polymorphisms. The allele frequencies show some regional differences, which, however, are statistically insignificant. In general the Turkish HP, GC, TF and PI allele frequencies do not differ obviously from those observed in other populations of Caucasoid origin.     

Thermodynamic and spectroscopic study of Cu(II) and Ni(II) binding to bovine serum albumin

The thermodynamics of Cu(II) and Ni(II) binding to bovine serum albumin (BSA) have been studied by isothermal titration calorimetry (ITC). The Cu(II) binding affinity of the N-terminal protein site is quantitatively higher when the single free thiol, Cys-34, is reduced (mercaptalbumin), compared to when it is oxidized or derivatized with N-ethylmaleimide. This increased affinity is due predominantly to entropic factors. At higher pH (approximately 9), when the protein is in the basic (B) form, a second Cu(II) binds with high affinity to albumin with reduced Cys-34. The Cu(II) coordination has been characterized by UV-vis absorption, CD, and EPR spectroscopy, and the spectral data are consistent with thiolate coordination to a tetragonal Cu(II), indicating this is a type 2 copper site with thiolate ligation. Nickel(II) binding to the N-terminal site of BSA is also modulated by the redox/ligation state of Cys-34, with higher Ni(II) affinity for mercaptalbumin, the predominant circulating form of the protein.     

Linkage mapping of AFLP and microsatellite DNA markers with the body color- and sex-determining loci in the guppy (Poecilia reticulata)

The guppy is an ornamental fish species that exhibits various phenotypic characteristics, such as body color and fin-shape. Although linkage relationships of a limited number of phenotypic traits have already been investigated, the association between phenotypic and molecular markers is still unknown. We constructed a total of 35 linkage groups for the guppy using 186 polymorphic loci of AFLP and microsatellite DNA. The locus related to the yellow body color was linked with ten markers and the sex-determination locus was linked with five markers.     

Proton relaxation studies in H 2 O-D 2 O mixtures. The binding of manganese (II) to bovine serum albumin

We have used the direct method for determining longitudinal relaxation times of water protons in H₂OD₂O mixtures. The relaxation time of pure water (2.7 sec) increases to 9.0 sec in 10% H₂O-90% D₂O mixture. This larger relaxation time enables us to use the direct method to accurately determine relaxation rate enhancements due to paramagnetic metal ions. The binding parameters for the interaction of manganese(II) to bovine serum albumin determined by this method are in excellent agreement with those determined earlier using pulsed methods.     

Linkage of isozyme loci in the mouse: Phosphoglucomutase-2 (Pgm-2), mitochondrial NADP malate dehydrogenase (Mod-2), and dipeptidase-1 (Dip-1)

The linkages of the isozyme genes Mod-2, Pgm-2, and Dip-1 have been determined in tests with established linkage group markers among inbred strains of mice. Unique alleles for both Mod-2 and Pgm-2 have been observed in the strain of SM/J. Linkage was determined from backcross progeny of the matings C57BL/6J×(SM/J×C57BL/6J)F₁, (SM/J×SWR/J)F₁×SM/J, and (SM/J×SWR/J)F₁×SJL/J. The gene Mod-2 is on linkage group 1. In a three-point cross of the loci Gpi-1, c, and Mod-2, the c locus was determined to be the middle gene. No double crossovers were observed. Our combined data show the following linkages: Gpi-1 to c, 28.3±3.2%; Gpi-1 to Mod-2, 33.3±3.0%; and c to Mod-2, 4.1±2.8%. The proposed gene order for four markers on LG I is Gpi-1-p-c-Mod-2. The gene Pgm-2 was linked to Gpd-1 (27.0±4.2%) on LGVIII. Two backcrosses segregating for Pgm-2 and b, (SM/J×DBA/2J) F₁×DBA/2J and (SM/J×DBA/2J)F₁×C57BR/cdJ, showed 9.1±4.3% recombination. The proposed gene order on LG VIII is b-Pgm-2-Gpd-1. The genes Pgm-1 and Pgm-2 are not linked (53.4±4.4%). Linkage of the isozyme genes Dip-1 and Id-1 on LG XIII was observed in backcross progeny of the crosses (SJL/J×C57BL/6J)F₁×SJL/J and C57BL/6J×(SM/J×C57BL/6J)F₁. The combined recombination was 23.8±2.8%. Two cases are established where genes whose enzyme products share substrate affinities (Pgm-1 and Pgm-2; Mod-1 and Mod-2) are not linked. Our data generally support the conclusion that functionally or metabolically related isozyme genes are not contiguous on mouse linkage groups.This investigation was supported in part by Public Health Service General Research Support Grant GM-09966 and in part by Public Health Service Training Grant 5T01 HD-00032-07 from the National Institute of Child Health and Human Development, and by Atomic Energy Commission contract AT(30-1)-3671.     

Interactions between bovine serum albumin and gemini surfactant alkanediyl-alpha, omega-bis(dimethyldodecyl-ammonium bromide)

Interactions between bovine serum albumin (BSA) and cationic gemini surfactant alkanediyl-alpha,omega-bis(dimethyldodecyl-ammonium bromide) (12-n-12, n=3, 4, 6) in aqueous solution have been investigated by measuring fluorescence, UV-vis transmittance, dynamic lighting scattering, and circular dichroism. Compared to a traditional surfactant dodecyltrimethylammonium bromide (DTAB), 12-n-12 interacts with BSA more strongly. With increasing concentration, 12-n-12 first binds specifically onto BSA leading to the unfolding and aggregation of BSA, and the decrease in alpha-helix content; and then forms micelle-like complexes along the unfolded BSA chains. A gemini surfactant with a longer spacer has a larger effect on BSA unfolding due to a stronger hydrophobic interaction.