Genetic polymorphism of transferrins in yaks and local cattle in Gorny? Alta?]

The object of this investigation was the genetic polymorphism of transferrins in Altaian and Mongolian yaks and in the aboriginal cattle of high-mountain regions of the Altai Territory. Both in the cattle and in yaks the usual 4-allele system of the transferin locus with a peculiar frequency and distribution of genotypes was found. A high frequency of occurrence of transferrin types D1 and D2 under the conditions of a severe pressure of natural selection suggests the existence of a correlation between the TF-genotypes and the adaptive capacities of the given cattle species.     

Foetal and neonatal development of evoked responses in guinea-pig auditory cortex.

Development of the response of the auditory cortex to unilateral acoustic stimulation by a chick was studied in guinea-pig foetuses from the 50th day to the end of gestation and in newborn animals. The first cortical response appeared on the 52nd to 53rd day of gestation. The maximum responses were concentrated in the temporal cortex, between the somatosensory (parietal) and optic (occipital) area. The progressive development of the latent period of the cortical response and of its various components distinctly slowed down on the last days of gestation. At the same time, the amplitude of the cortical response was temporarily augmented. The cortical response developed from a simple negative wave in the youngest embryos into an intricate complex with an initial positive component in newborn guinea-pigs. The basic components of this complex were already discernible on the 64th to 65th day of gestation. The ability to react to repeated peripheral stimulation of 0.1-2 c/s frequency increased with foetal age, with temporary deterioration on the last days of gestation. Resistance of the cortical auditory response to cerebral anoxia rose up to term, with a temporary drop from the 64th day of gestation. After the initiation of independent respiration, cerebral hypoxia and bilateral vagotomy chiefly influenced the stability of the more recent components of the cortical auditory response in mature foetuses.     

转铁蛋白的研究与发展

转铁蛋白(Transferrin,Tf,又称为铁传递蛋白、运铁蛋白)是一种重要的β球蛋白,是脊椎动物体内铁的运输者。自1945年Holmberg和Laurell首次在人血清中发现这种非血红素结合铁的转铁蛋白以来[1],人们又在猪等其它哺乳动物以及鱼类、两栖类及爬行类的血清中发现了Tf的存在[2],随后又相继发现了乳Tf和卵Tf以及Tf的蛋白类似物。由于Tf具有特殊的生理功能,Tf的研究一直受到国际上生命科学工作者的关注,人们已对许多种属Tf的结构与功能做了大量研究。     

Ethoxyformylation and photooxidation of histidines in transferrins

The chemical reactivity of histidines in ovotransferrin and human serum transferrin was studied utilizing two different reactions. Upon dye-sensitized photooxidation of ovotransferrin and ethoxyformylation of human serum transferrin and ovotransferrin, losses in histidine and iron-binding activity were observed. All of the histidines in both apoproteins could be ethoxyformylated by the use of 170 to 400 molar excesses of reagent resulting in complete loss in activity. The histidines of human serum transferrin showed a greater reactivity toward the reagent than did those of ovotransferrin. The binding of each iron protected two histidines from ethoxyformylation, and in both cases the proteins remained completely active. First-order losses in histidine and iron-binding activity were observed when ovotransferrin was irradiated in the presence of methylene blue. Comparison of the first-order rates indicates the loss of two histidines per binding site accounts for the inactivation of the protein. However, iron binding did not protect ovotransferrin from photoinactivation as expected. Evidence from both modification technqiues indicates: (1) Histidines are essential for iron-binding activity. (2) There are two essential histidines in each binding site. The advantages of using two modification reactions, ethoxyformylation and photooxidation, in the study of the functional role of histidines in proteins are demonstrated in this work.     

Comparative ultrastructure of Clara cells in neonatal and older cattle

Calf lungs were fixed with glutaraldehyde and examined by scanning (SEM) and transmission (TEM) electron microscopy to compare the ultrastructure of Clara cells in terminal bronchioles of neonatal calves and older cattle. In the neonatal calf, SEM revealed numerous smooth-surfaced Clara cells protruding above a similar number of ciliated cells, whereas in older animals the surface of Clara cells was lobulated. Thin sections examined by TEM revealed numerous cuboidal to columnar Clara cells with indented nuclei and a pale cytoplasm filled with faintly granular glycogen in the neonatal calf. Some cells were characterized by apical dense and/or pale membrane-bound granules or secretory droplets. Many cells had an apical tubular network of cisternae that were partly smooth and partly decorated with ribosomes. Ultrastructural comparison of Clara cells in a 2-day-old calf with those of 14- and 19-day-old, 4- and 5. 5-month-old, and 3.5-year-old cattle revealed a striking reduction in the amount of glycogen per cell after 14 days. The number of cells with apical granules was small at all ages, and the density of the secretory granules varied greatly in different cells. A variable amount of smooth endoplasmic reticulum (SER) was present but was less prominent than cisternae of ribosomal endoplasmic reticulum (RER). In older cattle, the limited amount of SER compared to the RER and secretory granules suggests that bovine Clara cells are more likely to be secretory than detoxifying.     

Specificity of chicken and mammalian transferrins in myogenesis

Chicken transferrins isolated from eggs, embryo extract, serum or ischiatic-peroneal nerves are able to stimulate incorporation of [3H]thymidine, and promote myogenesis by primary chicken muscle cells in vitro. Mammalian transferrins (bovine, rat, mouse, horse, rabbit, and human) do not promote [3H]thymidine incorporation or myotube development. Comparison of the peptide fragments obtained after chemical or limited proteolytic cleavage demonstrates that the four chicken transferrins are all indistinguishable, but they differ considerably from the mammalian transferrins. The structural differences between chicken and mammalian transferrins probably account for the inability of mammalian transferrins to act as mitogens for, and to support myogenesis of, primary chicken muscle cells.     

Genetic polymorphism of transferrins in Bovinae

Variability of transferrins in Bovinae is controlled by two loci: Tf (the locus of structural transferrin gene) and T (the locus of a gene responsible for protein modification). Originally, the ancestors of Bovinae, like the other ruminants, had the R type of transferrin (T-/T- genotype, inactive T gene). Later on, the T gene activation occurred and the B type appeared (T+/T-, T+/T+ genotypes). The subsequent evolution of Bovinae was accompanied by almost complete fixation of T+ allele. In one of the Bovinae representatives (Bos taurus L.) the frequency of T- allele remained at the level of approx 0.1. A hypothesis is proposed which explains the change of the transferrin type in Bovinae by imitation of multiple allelic forms of this protein present in Tf heterozygotes, by supplementary modificatory multiple transferrin forms arising on activation of the minor gene (T+). This process is assumed to involve the reduction of Tf locus variability. Since this hypothesis proceeds from the assumption of TF heterozygote advantage, the question is considered, whether this assumption is compatible with high polymorphism of Tf locus which significantly exceeds that for other loci.     

Differences between human and rabbit transferrins

Rabbit reticulocyte incorporation of iron from rabbit transferrin was independent of transferrin iron saturation but uptake from human transferrin was saturation dependent. Unlike human transferrin, rabbit transferrin does not surrender its iron from any unique preferred iron-binding site and can be described as functionally homogeneic.The two proteins also differ in their acid-base iron-binding properties. One human transferrin iron binding site retains an ability to bind iron at somewhat acid pH but this property is not shared by rabbit transferrin.     

Differences between human and rabbit transferrins.

Rabbit reticulocyte incorporation of iron from rabbit transferrin was independent of transferrin iron saturation but uptake from human transferrin was saturation dependent. Unlike human transferrin, rabbit transferrin does not surrender its iron from any unique preferred iron-binding site and can be described as functionally homogeneic. The two proteins also differ in their acid-base iron-binding properties. One human transferrin iron binding site retains an ability to bind iron at somewhat acid pH but this property is not shared by rabbit transferrin.