Partial purification and some properties of a nucleoside phosphotransferase of chick embryos

Summary A nucleoside phosphotransferase purified about 40fold from chick embryos utilizes efficiently as phosphate donors deoxyribonucleoside and pyrimidine ribonucleoside monophosphates, whereas the pyrimidine deoxyribonucleoside appear to be the preferred acceptors of phosphate. The enzyme is very unstable to heat, dilution and dialysis. A marked enhancement in the stability is caused by nucleotides and it seems associated with the formation of an aggregated state of the protein.     

Partial purification of a plasma-kinin-forming enzyme from horse urine

Zusammenfassung Durch Chromatographie mit Diäthylamino-äthyl-cellulose nach Ammoniumsulfat-Fraktionierung wurde ein Plasma-Kinin-freisetzendes Ferment aus Pferdeharn teilweise (80×) gereinigt. Das so gereinigte Präparat war gegen Pferde-, Menschen-, Rinder (Fraktion IV-4)- und Ratten-Blutplasma, nicht aber gegen Schweine-(Fraktion IV-4)-Globuline wirksam. Durch Sojabohnen-Trypsininhibitor oder Ovomucoid erfolgt keine Hemmung. Präparate von verschiedenem Reinheitsgrad zeigten entsprechendep-Toluenesulfonyl-l-arginin-methylester-spaltende und Kinin-freisetzende Wirksamkeit.

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Read before the XIIth Annual Meeting of the Sociedade Brasileira para o Progresso da Ciência, Piracicaba, July 1960; supported by Grant No. 58217 from the Rockefeller Foundation.     

Partial purification and characterization of acid phosphatase from sporulated oocysts ofEimeria tenella

Summary Acid phosphatase ofEimeria tenella oocysts (Peak II) was purified 77-fold with a recovery of 26% using protamine sulfate precipitation, DEAE-cellulose chromatography and Sephadex G-200 gel filtration. This enzyme occurs in multiple forms as indicated by two peaks which can be separated by DEAE-cellulose chromatography and polyacrylamide gel electrophoresis. The partially purified enzyme has optimal activity at pH 4.5. With p-nitrophenyl phosphate the Km and V_max values for (Peak II) were 25 mM and 1.57 mol/min/mg protein, respectively. The enzyme (Peak II) ist strongly inhibited by Hg⁺⁺, Cu⁺⁺, iodoacetamide, fluoride and molybdate. Tartrate and other divalent metal ions have no effect on enzyme activity. The partially purified Peak II phosphatase is not a glycoprotein as it is not absorbed on concanavalin-A Sepharose and its treatment with bacterial neuraminidase does not alter its elution profile through DEAE cellulose.     

Partial purification and characterization of acid phosphatase from sporulated oocysts of Eimeria tenella

Acid phosphatase of Eimeria tenella oocysts (Peak II) was purified 77-fold with a recovery of 26% using protamine sulfate precipitation, DEAE-cellulose chromatography and Sephadex G-200 gel filtration. This enzyme occurs in multiple forms as indicated by two peaks which can be separated by DEAE-cellulose chromatography and polyacrylamide gel electrophoresis. The partially purified enzyme has optimal activity at pH 4.5. With p-nitrophenyl phosphate the Km and Vmax values for (Peak II) were 25 mM and 1.57 mumol/min/mg protein, respectively. The enzyme (Peak II) is strongly inhibited by Hg++, Cu++, iodoacetamide, fluoride and molybdate. Tartrate and other divalent metal ions have no effect on enzyme activity. The partially purified Peak II phosphatase is not a glycoprotein as it is not absorbed on concanavalin-A Sepharose and its treatment with bacterial neuraminidase does not alter its elution profile through DEAE cellulose.     

Inhibitory effect of exogenous histones on cellular growth and DNA synthesis in Chlamydomonas reinhardtii.]

The addition of exogenous histones to synchronous culture of Chlamydomonas reinhardtii, at the beginning of the cell cycle, leads to the death of the cells. The same amount of histones added in the middle of the cycle, only blocks the cell division. The mechanism of this inhibition effect of the histones could involve a block at the level of the chloroplast DNA replication.     

Partial purification and some characteristics of hamster molar alkaline phosphatase

Summary A rapid 3-step method is given to purify partially hamster molar alkaline phosphatase. Molecular weight was 50,200 and isoelectric point 3.7. The alkaline phosphatases in the mesenchymal and ectodermal parts of the tooth are probably identical.     

Partial purification of an endogenous elicitor from suspension-cultured cells of red bean,Vigna angularis

Brief irradiation with a germicidal UV lamp of cells of red bean,Vigna angularis, cultured in suspension in a quartz flask caused the release into the culture medium of an endogenous substance with elicitor activity, as well as the accumulation of isoflavone glucoside stress metabolites in the cells. The active compound was fractionated using phenylalanine ammonia lyase (PAL)-inducing activity in fresh cells as a marker. The elicitor active principle appears to be a low molecular weight (<2000 MW) water-soluble acidic oligosaccharide.     

Partial purification of components from fasting human blood serum which stimulate the forward migration of human spermatozoa

Summary Components from fasting human serum that could stimulate the forward migration of human spermatozoa were isolated by gel filtration on Sephadex G-25. The results suggest that these components may be used to enhance sperm forward migration and, hence, pregnancy rate in artificial insemination with husband's semen, (AIH) especially in cases where the sperm forward migration is not optimal.This work was supported by a grant from the World Health Organization.     

Isolation and purification of the penicillinase from mycobacteria

Résumé La pénicillinase des myocbacteries est précipitée par l'acide benzoïque. L'élution d'acide se fait parn-butanol. L'élimination des polysaccharides étant donné par la précipitation avec PAS la substance devienne mieux soluble. La crystallisation de l'enzyme est obtenue en forme de crysteaux hybrides avec du phosphate d'ammoniaque. L'analyse spectrophotométrique prouve l'absence d'impuretés, l'électrophorèse revèle une bande individuelle d'une motilité ralentie.     

Chromatographic purification,crystallization and study of vegetablel-alanine: 2-oxoglutarate-aminotransferase properties

Zusammenfassung l-Alanin-2 Oxoglutarataminotransferase aus Soya,Glycine hispida, wurde 230fach gereinigt und kristallisiert sowie einige physikalisch-chemische Eigenschaften (Michaelis Konstante, spezifische Wirkung, pH, Temperatureinfluss, ionale Wirkungen und Metaboliten) wurden studiert.     

Preliminary purification and dosages of the erythropoietic factor from ox-spleen.

The administration of ox-spleen homogenate, whether in rats made polycythemic by blood transfusion or in mice polycythemic by hypoxia, elicited a significant stimulatory effect on the rate of erythropoiesis. This activity remained unchanged even if the spleen, before being homogenized, was exhaustively washed with isotonic buffer pH 7.4 up to the total blood elimination.     

b-nucleic acid,and the initial step of deoxyribonucleic acid-degradation by deoxyribonuclease I

Zusammenfassung Feulgen fand, dass die Degradation der Desoxyribonukleinsäure durch Pankreatin keine Mononucleotide bildete, jedoch auf der Stufe der Oligonucleotide (b-Nukleinsäure) blieb. In dieser Mitteilung wird die b-Säure mit dem ersten Degradationsprodukt identifiziert, welches aus Nukleinsäure unter Einwirkung von DNase 1 gebildet wird, und der Verlauf der Nukleinsäure-Degradation wird ausführlich verfolgt.     

A new approach to preparation and purification of colostrokinin from bovine colostrum

Summary A simple and rapid method is reported for preparation and partial purification of colostrokinin from bovine colostral whey. The active substance obtained at the described stage of purification appears to be a basic polypeptide of low molecular weight. This peptide proved to be undestroyed by pepsin, only partially by trypsin and completely by papain.Acknowledgment. This research was partially supported by the Italian Ministry of Health.