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At least 19 recordsLinked to original sources
PubMedDate not supplied

Effect of maternal antibody on experimental infections of chickens with a type-8 avian adenovirus.

Mortality was 60% when chickens without detectable maternal antibody to avian adenoviruses were inoculated intra-abdominally with 10(6) plaque-forming units of AMG 5(2a), a type-8 avian adenovirus. Other results were macroscopic and microscopic lesions in a wide range of organs, statistically significant depression of body weights, AMG 5(2a) virus in the liver and feces, and high virus-neutralizing antibody titers to AMG 5(2a). The disease produced was similar to that described in a previous report of AMG 5(2a) infection of chickens, and similar to inclusion body hepatitis as described in the literature. In contrast, similar inoculation of chickens with maternal antibody to type-8 avian adenovirus resulted in no mortality, lesions in the liver only, no depression of body weight, AMG 5(2a) virus in the feces only, and relatively low virus-neutralizing antibody titers. During this study a hemorrhagic-aplastic anemia syndrome occurred in both AMG 5(2a)-inoculated and control chickens in one trial. Pathologic, virologic, and serologic findings indicated that the spontaneously occurring disease was not caused by an avian adenovirus.

Adenoviridae Infections↗
PubMed1978

Actins from mammals, bird, fish and slime mold characterized by isoelectric focusing in polyacrylamide gels.

Actins isolated from a variety of tissues and cultured cells were compared by isoelectric focusing in polyacrylamide gels in the presence of 9 M urea and 2% Nonidet P40. Actins isolated from muscle tissue with a sarcomeric structure like skeletal muscle and heart muscle invariably display, as previously shown, one single band with a pI of approximately 5.4 (alpha-actin) in isoelectric focusing gels. Actins isolated from mammalian or avian non-muscle tissue and cultured mammalian cells display two polypeptide bands (beta and gamma-actins) focusing at a slightly higher pH than alpha-actin as a closely spaced doublet. A gamma-like actin is the predominant species in chicken gizzard actin. However, this gamma-like form is not isoelectrically identical with gamma-actin from brain. These results are discussed in relation with the currently available amino acid sequence data known for different actins. Actin isolated from the liver of the electric fish Torpedo marmorata appears to consist of a single isoelectric species with an apparent isoelectric point similar to the beta-actin component of mammalian brain. The actin from the slime mold Physarum polycephalum shows only one single major band in isofocusing gels with an isoelectric point lower than that of alpha-actin.

Actins↗
PubMed1978

Localization of actin in Dictyostelium amebas by immunofluorescence.

Antibody prepared against avian smooth muscle actin has been used to localize actin in the slime mold, Dictyostelium discoideum. The distribution of actin in migrating cells is different from that in feeding cells. Migrating amebas display fluorescence primarily in advancing regions whereas feeding amebas show uniform fluorescence throughout. The reaction is specific for actin since the fluorescence observed is blocked when the antibody is absorbed by actin purified from avian skeletal muscle, human platelets, and Dictyostelium. These results, in addition to describing the distribution of actin in D. discoideum, demonstrate that actins from these diverse sources share at least one common antigenic determinant.

Actins↗
PubMed1978

Selective binding of antibody against gizzard 10-nm filaments to different cell types in myogenic cultures.

Antibody against the intermediate-sized filaments from gizzard smooth muscle was used to determine the presence or absence of reacting 10-nm filaments in different cell types. The antibody against gizzard 10-nm filaments reacted with filaments in cultured smooth muscle cells, skeletal myotubes and postmitotic skeletal myoblasts. It did not bind to the 10-nm filaments present in replicating presumptive myoblasts and fibroblasts, or the 10-nm filaments in spinal ganglion cells.

Animals↗
PubMedDate not supplied

Myoglobin-O2-saturation profiles in muscle sections of chicken gizzard and the facilitated O2-transport by Mb+.

It has been shown that the oxygen transport in intact muscle can be quantitatively determined using Mb as an oxygen indicator in the cryomicrophotometric method. 1) The influence of the parameters such as time, temperature, boundary PO2 and metabolism on the oxygen transport in sections of chicken gizzard could be quantitatively determined from measured MbsO2-profiles; 2) The MbsO2-profiles measured under various conditions can be reproduced using a mathematical model which considers not only the diffusion of dissolved O2 but also the facilitated diffusion as well as O2 consumption. From this mathematical results it can be concluded that the mobility of the Mb in the muscle cells is limited and that Mb in the PO2-region between 5 and 0 mmHg contributes to at most 40% to the total O2-transport in chicken gizzard.

Animals↗
PubMed1978

Striated myofibrils in anti-myosin stained, isolated chicken gizzard smooth muscle cells.

Highly purified chicken gizzard myosin was used to induce antibody production in rabbits. The IgG fraction was separated from the antisera and coupled to fluorescein isothiocyanate (FITC). Specific antibody (AGM) was isolated from the IgG fraction by affinity purification. Comparisons of the specificity of IgG and AGM for chicken smooth muscle myosin revealed a much greater specificity by AGM. Staining with IgG led to an apparent cross-reactivity with guinea pig smooth muscles which was not seen with AGM staining. Therefore, staining of cells for localization of myosin was performed with AGM. Isolated cells were obtained from chicken gizzards either by collagenase digestion or by agitation of glycerinated pieces. Stained cells and cell fragments revealed the presence of myofibrils as structural units with diameters of about 1.0 micrometer. Stained myofibrils occasionally displayed regular banding patterns with a repeating period of about 1.5 +/- 0.2 micrometer. The presence of banded myofibrils in non-cultured cells shows that the organization of the contractile material is similar to that previously reported for cultured cells by Gröschel-Stewart.

Animals↗
PubMed1979

Production of specific antibodies to contractile proteins and their use in immunofluorescence microscopy. III. Antiobody against human uterine smooth muscle myosin.

The preparation of highly purified myosin from surgical specimen of human uterine muscle is described. Antibodies were raised in rabbits against this immunogen. In immunodiffusion, they react with uterine and chicken gizzard muscle myosin, no reaction is observed between uterine myosin and the anti-chicken-gizzard- myosin. In immunofluorescence, anti-uterine-myosin stains smooth muscle in the contractile and "modulated" state and non-muscle cells such as fibroblasts, platelets and endothelium of various species. Thus, these antibodies contrast anti-gizzard-myosin, which has previously been shown to be specific for contractile state muscle cells. We therefore conclude that the uterine myosin preparation consists of two immunogens, the one being associated with cell contractility and the other, termed cytoplasmic myosin, with motility and mitosis. The latter is indistinguishable from the myosin present in non-muscle cells and can be absorbed specifically with actomyosin from blood platelets.

Animals↗
PubMed1976

Comparative studies on amino and thiol groups in myosins from different sources.

Myosins from rabbit white and red skeletal, rabbit heart, fish skeletal and chicken gizzard muscles, as well as from human platelets were subjected to trinitrophenylation by trinitrobenzene sulfonate and alkylation by N-ethylmeleimide which affected their amino and thiol groups, respectively. The blocking of amino groups was carried out in the presence or in the absence of Mg-ADP and was followed both spectrophotometrically and enzymatically. Essential amino groups, whose modification throughly changes the enzymic characteristics of myosin, were found in heart and in all skeletal muscle myosins but were absent in myosins from chicken gizzard muscle and from human platelets. The reaction of these amino groups was highly retarded in the presence of Mg-ADP. Alkylation of thiols led to loss of the K+-activated ATPase (ATP phosphohydrolase, EC 3.6.1.3) in all myosins. However, the rate of loss of activity varied from one myosin to another and, for a given myosin, was affected by the presence of nucleotides and by the value of the ionic strength. The change in Ca(2+)-activated ATPase activity (ATP phosphohydrolase, EC 3.6.1.3) on alkylation was influenced by the presence of Mg - ADP during the reaction. In the absence of this nucleotide, the Ca(2+)-ATPase activity increased and reached a plateau as a consequence of modification. The extent of activation largely depended on the origin of the myosin. When alkylation was carried out in the presence of Mg-ADP, the Ca(2+)-ATPase activity as a function of time exhibited a maximum but the descending part of the curve was absent in myosins from heart and gizzard muscles.

Adenosine Triphosphatases↗
PubMed1977

N- and C-terminal amino acids of purified alpha-actinin.

Highly purified bovine cardiac alpha-actinin is obtained by successive chromatography on DEAE-cellulose and hydroxyapatite of a crude fraction obtained by salting out low ionic strength extracts of bovine cardiac muscle between 0 and 30% ammonium sulfate saturation. Hydroxyapatite chromatography removes a 43 000-dalton polypeptide chain that is difficult to remove by successive DEAE-cellulose columns. Removal of all 43 000-dalton material by hydroxyapatite chromatography is accompanied by disappearance of a very small 9 to 10 S boundary in analytical ultracentrifuge diagrams of DEAE-cellulose-purified 6.2S alpha-actinin. Approximately 95% of the protein in DEAE-cellulose and hydroxyapatite-purified alpha-actinin is the 100 000-dalton alpha-actinin polypeptide as estimated by SDS-polyacrylamide gel electrophoresis. Purified bovine cardiac, porcine skeletal, chicken gizzard, and chicken breast alpha-actinins all contain leucine as the C-terminal amino acid of both polypeptide chains in the alpha-actinin molecule. Bovine cardiac and porcine skeletal alpha-actinins contain arginine as the amino acid penultimate to C-terminal leucine. None of the four different alpha-actinins studied had a N-terminal amino group available for reaction with dansyl chloride, but all four alpha-actinins contained 1.6 to 1.8 acetate residues per molecule (200 000 daltons) of alpha-actinin. It seems likely that the N-terminal amino groups of both polypeptide chains in these four alpha-actinins are acetylated. A peptide having the composition N-Ac-Asp2-Glu4 was isolated from a proteolytic digest of bovine cardiac alpha-actinin. alpha-Actinin seems to be a conserved protein molecule found in many different motile systems.

Actinin↗
PubMed1978

Light chains of chicken embryonic gizzard myosin.

1. Myosin from gizzards of 15-day-old chicken embryos was highly purified by ammonium sulfate fractionation in the presence of ATP and MgCl2, ultra-centrifugation and Sepharose 4B chromatography. 2. The myosin composed of heavy and three light chains as determined by sodium dodecyl sulfate (SDS) gel electrophoresis. The molecular weights of the light chains were 23,000 (L23), 20,000 (L20), and 17,000 (L17), respectively. The amount of L23 light chain decreased and disappeared, and the L17 light chain increased steadily in the course of development. The amount of L20 light chain did not change. 3. ATPase activity of the embryonic myosin was essentially the same as that of adult myosin. The change in the light chain pattern in the course of development did not correlate to the ATPase activity. 4. Antigenicity of the heavy chains in the embryonic myosin was the same as that of the adult heavy chains. However, antibodies to light chains were not detected in the antibodies to either the embryonic or adult myosins.

Adenosine Triphosphatases↗