Purification and immobilization of human carbonic anhydrase B by using polyacrylamide gel.

Human erythrocyte carbonic anhydrase B was purified and immobilized in polyacrylamide gel. As compared to the soluble enzyme, the immobilized enzyme was considerably more resistant to heat and sulphanilamide action.     

Calcifying bacteria and carbonic anhydrase]

Carbonic anhydrase activity was measured on bacteria known for their calcifying power. The results obtained allow us to conclude that carbonic anhydrase is not present in their enzymatic equipment. Nevertheless, the addition of carbonic anhydrase in culture media increases the growth of the cultures and their calcifying power. This result is due to the direct action of the enzyme on the pH of the culture medium. The results obtained could be applied to the mechanism of dental plaque calcification.     

Histochemical localization of carbonic anhydrase in fowl proventriculus

Summary The carbonic anhydrase activity in fowl proventriculus was studied by the histochemical method of Hansson. The activity was observed in the mucose membrane cells and in proventricular gland cells. These results, about which there is disagreement in the literature, are discussed in the text.     

Effect of physical exercise on the specific activity of carbonic anhydrase isozyme in human erythrocytes

Summary Significant decreases in the levels of both carbonic anhydrase type B and total esterase activity of human erythrocytes were observed after physical exercise (bicycle ergometer, 150 W for 30 min). Since carbonic anhydrase B-dependent esterase activity likewise decreased, the decrease in the total esterase activity would be caused by the decrease of carbonic anhydrase B activity. The specific activity of carbonic anhydrase B tended to decrease after the exercise. On the other hand no such effects were noted for carbonic anhydrase type C.     

Histochemical demonstration of carbonic anhydrase activity in mast cells

Zusammenfassung Carboanhydraseaktivität in Mastzellen der Ratte wurde mittels Modifikation der Methode vonHäusler ⁴ demonstriert. Kapillarendothel, Basalzellen des Zungenepithels und Muskelgewebe reagierten ebenfalls positiv.     

Immunological identification of human plasma3S_{\gamma _1 } -globulin as carbonic anhydrase

Résumé La -globuline, précédemment isolée du plasma humain normal, a fait l'objet d'une comparaison immunologique avec l'anhydrase carbonique B isolée à partir d'érythrocytes. L'immunoélectrophorèse en gélose et l'immunofluorescence analysée sur le tissu rénal ont montré l'identité immunologique de ces 2 protéines.     

Histochemical localization of carbonic anhydrase in Malpighian tubules ofCulex pipiens

Summary Carbonic anhydrase (CA) activity has been localized histochemically by Hansson's method in Malpighian tubules ofCulex pipiens. The enzyme has been observed on membranes of the cytoplasmic inclusions of Malpighian cells; no CA activity has been found in other cytoplasmic structures. The possible meaning of the localization of the enzyme is discussed.     

Separation of serum proteins in different amphibian species by polyacrylamide gel electrophoresis

Zusammenfassung Mittels Polyacrylamid-Gel-Elektrophorese wurden die Serumproteine von 11 Amphibienarten in 15 bis 20 Fraktionen aufgetrennt. Das elektrophoretische Muster wurde mit demjenigen des menschlichen Serums verglichen und erwies sich als artspezifisch.

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This investigation was supported by grants from the Schweizericher Nationalfonds zur Förderung der wissenschaftlichen Forschung and the Georges und Antoine Claraz-Schenkung.     

Purification of solubilized fucosyltransferase from lamb brain using ethylagarose gel]

The glycoprotein: fucosyl-transferase of the cerebral hemispheres, assayed with desialylated fetuin as exogenous acceptor, was the most active of the protein: glycosyltransferases tested in the brain. The addition of Titron X-100 to the membrane suspension, followed by high speed centrifugation, led to a solubilization of the enzyme. The use of hydrophobic chromatography on ethylagarose gave a good purification of this solubilized fucosyl-transferase, whose homogeneity has been shown by Ultrogel AcA 22, DEAE-cellulose chromatography and disc electrophoresis.     

Purification of the cytosol oestradiol-receptor complex from foetal guinea-pig uterus using electrofocusing on polyacrylamide plates

The 3H-oestradiol receptor complex obtained from the cytosol fraction of foetal guinea-pig uterus was purified by the following steps: column chromatography in Sephadex G-15 and Ultrogel, and by electrofocusing on polyacrylamide plates. In the final step a concentration of 15-17% of the foetal uterine oestradiol receptor protein was obtained. The isoelectric point (pl) of this receptor was determined to be 6.1-6.2.     

Purification of the cytosol oestradiol-receptor complex from foetal guinea-pig uterus using electrofocusing on polyacrylamide plates

Summary The³H-oestradiol receptor complex obtained from the cytosol fraction of foetal guinea-pig uterus was purified by the following steps: column chromatography in Sephadex G-15 and Ultrogel, and by electrofocusing on polyacrylamide plates. In the final step a concentration of 15–17% of the foetal uterine oestradiol receptor protein was obtained. The isoelectric point (pl) of this receptor was determined to be 6.1–6.2.The expenses of the investigation were partially defrayed by a grant from the Centre National de la Recherche Scientifique (CNRS), France (Equipe de Recherche CNRS No. 187).     

Mg2+-HCO-3-ATPase and carbonic anhydrase in rat intestinal mucosa

Mg2+-dependent and HCO-3-stimulated ATPase activity was highest in the brush border (microvilli) of rat duodenal mucosa compared with that of the other gastrointestinal mucosa. This ATPase may be useful to neutralize the gastric acid in the duodenal lumen. Carbonic anhydrase seems to accomplish a subsidiary role in the above reaction.     

Immunohistochemical localization of carbonic anhydrase C in the rat central nervous system]

With obtention of specific antibodies against isoenzyme C of Rat carbonic anhydrase it was possible to realize an immunohistochemical localisation in central nervous system of Rat. Results showed that this enzyme was mainly localized in cytoplasm of oligodendroglial cells and in low concentration in myelin sheath.     

Evidence for the existence of two carbonic anhydrase isozymes in rabbit ciliary body

Summary Two carbonic anhydrase isozymes were found in the rabbit ciliary body. Their isoelectric points were determined to be pH 6.6 and pH 7.4, respectively. The total activity of the higher isoelectric point isozyme was higher than that of the lower isoelectric point isozyme.     

Evidence for the existence of two carbonic anhydrase isozymes in rabbit ciliary body

Two carbonic anhydrase isozymes were found in the rabbit ciliary body. Their isoelectric points were determined to be pH 6.6 and pH 7.4, respectively. The total activity of the higher isoelectric point isozyme was higher than that of the lower isoelectric point isozyme.