ANALYSIS OF INTROGRESSIVE LINES OF INTER-SPECIES PEA HYBRIDS BY BAND COMPOSITION OF SEED PROTEINS

Background. The reproductive incompatibility of cultivated (Pisum sativum) and wild (P. fulvum) pea species determines the difficulties of obtaining hybrids as well as the transfer of valuable wild parent alleles into interspecific hybrids and their use in the breeding process. The aim of the research was a comparative study of protein spectra of pea interspecific hybrids BC2F5 P. sativum x P. fulvum obtained by the authors and their parents. Materials and methods. The band composition of seed proteins in the interspecific hybrids of peas BC2F5, variety Stabil (P. sativum) accession from VIR collection I-609881 (P. fulvum) has been studied. Effectiveness of parent gene transfer determining each polymorphic position of electrophoretic spectrum were evaluated. Results. The ratio of the actual frequencies of the bands of the cultivated and wild parents in the introgression lines corresponded to the expected level in 73% of the positions of the electrophoretic spectrum. The introgression rate of individual seed protein bands from wild parent into interspecific pea hybrids in the absence of selection significantly exceeded the expected level, which may indicate the adaptive value of alleles encoding unique seed protein isoforms. Conclusion. The possibility of introgressive transfer of wild-type alleles to the cultivated genotypes of pea, as well as the presence of identified cultivated isoforms of storage proteins in all studied lines of BC2F5 interspecific hybrids in 88.2% of the polymorphic positions of the electrophoretic spectrum, indicates the possibility of using the wild species P. fulvum in pea breeding.

Polymorphism of storage proteins of common backwheat (Fagopyrum esculentum Moench.) in groups of varieties with different flower color

Aim. To establish the presence of polymorphism and differences in variants of the protein spectrum of buckwheat seed storage proteins in groups of varieties with different colors of the flower corolla. Methods. Electrophoresis using the Laemmli method in 17.5% of the separating PAAG gels, visualization and identification of the spectrum variants. Results. The common variants of the electrophoretic spectrum for all groups of buckwheat varieties and the heterogeneity of each of the studied groups of genotypes are revealed. By frequency of variants of electrophoretic spectrum between groups of varieties were detected statistically significant differences and reliable predominance of individual variants in green-flower morphotypes of buckwheat were established. Conclusions. Differences in frequency of occurrence of variants of electrophoretic spectrum in different morphotypes of buckwheat indicate the probable processes of preservation of individual adaptive alleles of genes of seed storage proteins, which occurred in populations when varieties under the pressure of breeding process. Keywords: edible buckwheat, spare proteins, globulins, albumins, polymorphism.

Specific Analysis of Immunoglobulins. Techniques and Clinical Value

We recommend that routine screening of sera for immunoglobulin disorders consist of a combination of electrophoresis in agarose and immunochemical quantitation of serum IgG, IgA, and IgM. Abnormalities detected by this procedure may be classified as (a) immune deficiencies, (b) polyclonal hyperimmunoglobulinemias, or (c) monoclonal immunoglobulin disorders. The analyst can contribute to the diagnosis of immune deficiency by detecting evidence for plasma protein losses in the urine, unsuspected monoclonal immunoglobulin disorders, and abnormalities in the immunoglobulin content and spectrum of secretions. Polyclonal hyperimmunoglobulinemia —seen in infections, autoimmune disease, liver disease, sarcoidosis, or other conditions—is frequently associated with an imbalance between the different immunoglobulin classes, and with the appearance of discrete inhomogeneities in the immunoglobulin zones of the electrophoretic spectrum. Factors involved in this process are listed, and examples are indicated. Monoclonal immunoglobulin disorders may not be detected if the tumor protein is masked by normal serum-protein fractions or misdiagnosed by confusion with nonimmunoglobulin components. Diagnosis of immunocyte malignancy is aided by detection of Bence Jones protein in the urine; measurements of serum IgG, IgA, and IgM concentrations; and monitoring the concentration of the abnormal component in the serum as the disease evolves.

INFLUENCE OF STRESS AND ENDOCRINE FACTORS ON PLASMA PROTEINS IN THE RAT

ABSTRACT The effects have been studied in albino rats of experimental stress, adrenalectomy, hypophysectomy and somatotrophin (STH) on the relative serum protein fractions, as determined from estimations of serum protein concentrations and the results of paper electrophoretic separation. In addition, the absolute amounts of serum proteins obtained from concurrent electrophoretic separation, estimation of serum protein concentration and determination of plasma volume were studied. It appeared inter alia that hypophysectomy gave rise to a reduction in the absolute amount of serum proteins, which was due to a reduction in the albumin + alpha1 globulin fraction while the other globulin fractions remained unaffected. STH administration caused an increase in both the albumin and globulin fractions in hypophysectomized rats. Formalin stress was accompanied by changes in the electrophoretic spectrum suggesting an increased globulin synthesis. Since stress is known to give rise to a proliferation of the lymphoid organs which, at least to some extent, is caused by STH we consider it justifiable to conclude that the probable enhancement of globulin synthesis accompanying stress is due to the action of STH.