The effect of organic phosphates on the oxygen equilibrium function of hemoglobin M Iwate.
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Biomedical subjects
Publications and source records attributed to K Imai.
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The oxygen binding properties of Hb M Hyde Park (92 beta, histidine leads to tyrosine) were reinvestigated directing special care to testing the wave length-dependence of the oxygen equilibrium curve and to stabilizing hemoglobin samples using a methemoglobin reductase system. There was no indication that the Hb M Hyde Park fraction separated on a DEAE Sephadex column contained an unknown hemoglobin derivative which appeared in earlier studies. Contrary to earlier observations, there was no significant wave length-dependence of the equilibrium curve of Hb M Hyde Park, verifying the spectrophotometric determination of oxygen saturation. The reductase system satisfactorily reduced the normal alpha chain met hemes without reducing the abnormal beta chain met hemes. The oxygen binding property of Hb M Hyde Park is characterized by 3 to 4 times higher oxygen affinity than that for normal hemoglobin, complete loss of cooperativity, and substantially preserved Bohr effect. These results are consistent in part but not entirely with those observed by earlier investigators. The oxygen affinity of Hb M Hyde Park is between the affinity of the oxy structure and the deoxy structure of normal hemoglobin. Oxygen equilibrium curve of red cell suspension and whole hemolysate containing Hb M Hyde Park were biphasic, indicating that Hb M Hyde Park also exhibited the high oxygen affinity in those samples.
The vascular responsiveness and the body fluid distribution were studied in 5 hypotensive and 11 normotensive patients on long-term hemodialysis. A diminished vascular responsiveness to intravenously infused norepinephrine or angiotensin II was found in uremic patients, especially in the hypotensive group. A slightly larger, but non-significant circulating blood volume (CBV) and a less extracellular fluid volume (ECF) was found in the hypotensive group as compared with those of the normotensive group. These results suggest that with autonomic nervous dysfunction, such a diminution of vascular responsiveness may be an another factor responsible for the development of hypotension.
The homogeneous acellular materials in the adenomatoid odontogenic tumor, calcifying epithelial odontogenic tumor, and calcifying odontogenic cyst were examined histochemically for specific staining of amino acids and protein groups. These materials gave a positive reaction for periodic acid-Sciff (PAS), alloxan-Schiff, and dinitrofluorobenzene-H-acid and low reaction for alcian blue, dimethylaminobenzaldehyde (method for tryptophan) and the Morel-Sisley diazotization method. They appear to have approximately the same composition as enamel matrix and are not amyloid in nature. The materials may be synthesized products from neoplastic epithelium that may originate from enamel organs.
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The indirect rosette assay which detects the interaction of antibodies with target cells by their ability to rosette with sheep red blood cells chemically coated with purified anti-immunoglobulin antibodies or with protein A from Staphylococcus aureus has been used to analyze xenoantisera to human melanoma-associated antigens. The test has been developed as a microassay and performed in microtiter plates, thus facilitating the screening of large numbers of samples. When modified as an inhibition assay, the assay has been successfully used (a) to compare the specificities of xenoantisera elicited with cultured melanoma cells, hybrids derived from the fusion of cultured human melanoma cells, and murine fibroblasts and melanoma-associated antigens purified by biochemical procedures and (b) to investigate the relationship of melanoma-associated antigens with beta 2-microglobulin and HLA antigens on the membrane of melanoma cells.
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A microbiological method for quantitative determination of cefadroxil in biological specimens is described. This method is essentially a cylinder-plate or a paper-disc method using Micrococcus luteus ATCC 9341 as the test organism grown in the tryptosoya broth added with 1.5% agar. Cefadroxil standard calibration curves are prepared in pooled human serum, moni-trol I or consera for the determination of serum level of human, and 0.1 M phosphate buffer (pH 6.0) to determine urine level. Cefadroxil in human serum and urine specimens can be measured by cylinder-plate method as low as 0.16 approximately 0.31 micrograms/ml and 0.08 approximately 0.16 micrograms/ml, respectively. Further, any active metabolites of cefadroxil were not detected on human and rat urine specimens by bioautography.
1. Human serum protein binding of cefadroxil and some other cephalosporins were determined by centrifugal ultrafiltration (U.F.) method and equilibrium dialysis (E.D.) method. The binding rates of cefadroxil were 28.1% by U.F. method and 3.8% (beta 1*), 11.6% (beta 2*) by E.D. method. 2. Protein binding of cefadroxil with sera of various animal species were also determined by E.D. method. The binding rates were low as well as that with human serum. 3. With two popular calculation formula for E.D. method, binding rate was considered on the alteration of the ratio of V2/V1.
A single dose 50 mg/kg of cefadroxil was administered orally to rats in fasting and non-fasting. In both fasting and non-fasting, the serum levels of cefadroxil were higher than those of cephalexin. In fasting, the biological half-life (T 1/2) of cefadroxil was longer than that of cephalexin. This indicates its prolonged durable action. Ingestion of cefadroxil with food affected the serum level less than that of cephalexin with food, and the serum levels of cefadroxil in non-fasting were same as those of cephalexin in fasting.
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