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A Kubicz

Publications and source records attributed to A Kubicz.

33 records · Page 2Linked to original sources
PubMed1979

Partial purification and some properties of a liver alkaline ribonuclease from the frog Rana esculenta.

1. RNAases varying in pH optimum, activation with pCMB, sensitivity towards temperature and acid treatment, as well as electrophoretic mobility were found in Rana esculenta liver extract. 2. Of the three activity peaks of alkaline ribonuclease separated on CM-cellulose with 2000-fold purification, RNAase of peak C is thermo- and acid-stable and exhibits specificity for pyrimidine bases, preferring poly(U) over poly(C). 3. Differences in the specific "inhibitory effect" of frog liver supernatant on the frog liver alkaline RNAase were observed.

Animals↗
PubMed1978

Acid phosphatase from liver of the frog Rana esculenta, separation and partial characterization of multiple forms.

1. Acid phosphatase (AcPase) from liver of the frog, Rana esculenta has been isolated and purified. The enzyme is heterogeneous, showing 4 activity zones on disc electrophoresis. The AcPase was separated into 3 peaks on DEAE-cellulose. Peak A corresponding to the electrophoretic AcPase IV represents an extensively purified enzyme form. 2. The separated enzyme forms are change isomers with a molecular weight of about 33,000. They differ markedly in substrate requirements and sensitivity towards activators and inhibitors. All of them are highly activated by dithiothreitol, show a rather restricted substrate specificity, and marked activity against ATP.

Acid Phosphatase↗
PubMedDate not supplied

Spontaneous conversion of carp liver AcPase I and some properties of its asialo-form.

Evidence is given for a spontaneous conversion of AcPase I to a more basic form due to autolytic loss of sialic acid. To investigate whether the presence of sialic acid in the enzyme molecule is of any physiological significance some physico-chemical properties of an enzymatically obtained asialo-AcPase I were studied. It has been shown that the asialo-form retained the properties of the native enzyme in respect to thermostability and pH-stability but modified slightly the hydrolytic activities of some phosphorylated compounds, and this might be of significance under physiological conditions.

Acid Phosphatase↗
PubMedDate not supplied

The RNAse-RNAse inhibitor system in the liver of the frog Rana esculenta: subcellular distribution and differential binding of inhibitor with multiple RNAses.

The aim of our work was to investigate the biological basis of the existence of multiple alkaline RNAses in the Rana esculenta liver with respect to formation of a RNAse-RNAse inhibitor complex (latent RNAse). Subcellular distribution indicated that most of the alkaline RNAse activity appeared in the high-speed supernatant and mainly in a latent form bound to an endogenous inhibitor. This RNAse-RNAse inhibitor complex was isolated, the bound RNAse activity was released and found to correspond to RNAse III and RNAse IV, the two most cathodic RNAses present in the supernatant fraction. The two RNAses differed markedly in the ability to interact with the inhibitor and this might be essential for the different biological roles the RNAses may play in the regulation of cytoplasmic RNA level. On the basis of molecular weight determinations we assume that the enzyme-inhibitor complex is shared by two different RNAses.

Animals↗