Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.5.1.4 (deaminase)
 5,113 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

1. Alanine inhibits rabbit muscle AMP-deaminase while aspartate, histidine and glutamate are ineffective. 2. The degree and type of inhibition of AMP-deaminase by alanine depend on pH; at pH 6.5 alanine behaves like an allosteric effector exerting a negative heterotropic effect. At pH 7.0 the inhibition is non-competitive, Ki being as high as 19 mM. 3. The probable significance of the effect of alanine on AMP-deaminase in muscle metabolism is discussed.
Acta Biochim Pol 1976
PMID:Inhibition by alanine of AMP-deaminase from rabbit skeletal muscle. 0 58

A method was elaborated for obtaining polyacrylamide gel zymograms of the cobalt-activated acylase after electrophoresis. Two fractions of the acylase showing activity towards N-chloroacetyl-gamma-L-glutamyl-beta-naphthylamide were found in human kidney, liver and intestine. The two fractions isolated from liver differ in substrate specificity, heat resistance, response to metal ions, inhibition by deaminated dipeptides, and in molecular weight. They differ also from other N-acylamino acid amidohydrolases: aminoacylase (EC 3.5.1.14) and aspartoacylase (EC 3.5.1.15).
Acta Biochim Pol 1978
PMID:Polymorphism of the cobalt-activated acylase in human tissues. 2 51

alpha-Hydroxyisocaproyltyrosine (HyIc-Tyr-OH), a potent competitive inhibitor of the cobalt-activated acylase form 2, was synthesized. Its derivative, alpha-aminopentyl-HyIc-Tyr-OEt was coupled to cyanogen bromide-activated Sepharose 4B and was used for about 100-fold purification of the acylase from human liver by affinity chromatography. The preparation obtained did not show aminoacylase, aspartyl acylase or alanylarylamidase activities. The same chromatographic method was also applied to isolate form 2 of the serum acylase from patients with viral hepatitis and guinea pig placenta.
Acta Biochim Pol 1979
PMID:Purification of cobalt-activated acylase by affinity chromatography. 57 48

The activity of cobalt-activated acylase, measured towards N-chloroacetyl- and N-butyryl-gamma-L-glutamyl-beta-naphthylamide, was found in all tissues of the adult animals. In the kidney, liver and small intestine of adult guinea-pig and rat two fractions differing in electrophoretic mobility (fractions 1 and 2) were present. The early foetus contained fraction 2, sometimes accompanied by fraction 3 which later disappeared; on further development of the foetus, fraction 1 appeared. Fraction 1 was distinctly activated by cobalt ions; fractions 2 and 3 were strongly inhibited by deaminated leucylphenylalanine. In the guinea-pig, the molecular weight of the three fractions ranged from 43000 to 59000.
Acta Biochim Pol 1978
PMID:Activity and polymorphism of the cobalt-activated acylase in tissues of rodents during development. 66 76

1. AMP-deaminase (AMP-aminohydrolase, EC 3.5.4.6) from rabbit skeletal muscle showed sigmoid-shaped plots of velocity versus substrate concentration at four temperatures tested between 15 degrees and 35 degrees C. In the presence of 20 mM-KCl, the plot was sigmoid only at 30 degrees C and became hyperbolic at the other temperatures tested. In the presence of 150 mM-KCl the plots were hyperbolic at all the temperatures applied. 2. The Km value depended on temperature and concentration of KCl, whereas Vmax was the same for the 20 mM- and 150 mM-KCl-activated enzyme. 3. The value of enthalpy of the enzyme-substrate complex formation was the same for both the 20 mM- and 150-mM-KCl-activated enzyme at lower temperature range (less than 38 degrees C), whereas at higher temperatures (greater than 38 degrees C) this value was much more negative in the presence of 20 mM-KCl than of 150 mM-KCl.
Acta Biochim Pol 1976
PMID:Potassium-dependent thermal sensibility of AMP-deaminase from rabbit skeletal muscle. 97 34

AMP-deaminase from cow uterine smooth muscle has been purified. The enzyme activity is regulated by the two cooperating mechanisms: allosteric and dissociation--association.
Acta Biochim Pol 1991
PMID:Isolation and regulatory mechanisms of smooth muscle AMP-deaminase. 179 1

In chronic renal failure AMP-deaminase operates in the erythrocytes at a much higher velocity than in healthy subjects, with a simultaneous shift from the AMP-adenine-inosine-hypoxanthine pathway (55% and 19%, respectively) to the pathway initiated by AMP-deaminase (45% and 81%, respectively).
Acta Biochim Pol 1990
PMID:Degradation of adenine nucleotides in the erythrocytes of patients with chronic renal failure. 208 6

The Swatek's method was further simplified for the assay of penicillin amidase activity. The absorbance of colour obtained during determination of 6-aminopenicillanic acid was dependent on concentration of 4-dimethylaminobenzaldehyde and on temperature. Antiodies induced in rabbits with one molecular form of penicillin amidase from E. coli PCM 271 (PA-1 or PA-2) did not cross-react with the other amidase form. No differences in substrate specificity on inactivation with SDS and in alkaline medium between the two amidase forms were observed. Concentrated urea inactivated PA-2 irreversibly and PA-1 reversibly. N-Bromosuccinimide inactivated almost completely only PA-1. Two E. coli PCM 271 strain variants were separated by microbial selection. Each of them produced only one amidase form. Also two amidase forms were found in cells of E. coli ATCC 11105, whereas E. coli ATCC 9636 and ATCC 9637 synthesize only PA-1.
Acta Biochim Pol 1987
PMID:Two molecular forms of penicillin amidase synthesized by Escherichia coli. 283 78

The activity of cobalt-activated acylase was determined in the serum of mice with transplantable leukemia (P 388, L 1210 standard, L 1210/ara-C, L 1210/CH3-G, plasmocytoma ADJPC-5, lymphoma AKSL-4 and natural leukemia in mice NZB). A statistically significant increase in enzyme activity in all leukemias except lymphatic leukemia has been demonstrated. The results suggest possibility of using the enzymatic measurement as a marker of transplantable leukemia in mice.
Pol Arch Weter 1988
PMID:Serum cobalt-activated acylase as a marker of transplantable leukemia in mice. 327 96

AKR mice highly susceptible to leukemia were fed orally for 9 months every days with a water solution of peat-liking preparation PF-290/II/2 at a dose 0.2 cm3 (70 g/cm3 water). After bleeding body and internal organs weight were measured and their ratio were calculated. Anatomo-pathological lesions, histopathological and ultrastructural examinations with the use of transmission and scanning microscope, serum cobalt-activated acylase (AA-Co) activity and urine arylsulphatase (ASA) activity were performed. It was found used preparation had some anti-tumors effect of mice with lymphatic leukemia. Serum cobalt-activated acylase and urine arylsulphatase of AKR mice for observation on disease development and dynamics of this process. In the ultrastructural picture changes of lymphatic cells after outside removal of degradated complexes of intracell membranes was observed.
Pol Arch Weter 1987
PMID:[Morphological and biochemical studies of the effect of the peat-derived preparation PF-290/II/2 on the development of natural lymphatic leukemia in mice]. 348 32


1 2 3 Next >>