Properties of Rat Liver L-Threonine Deaminase

1994 ◽  
Vol 48 (2) ◽  
pp. 90-97 ◽  
Author(s):  
Roberto Pagani ◽  
Roberto Leoncini ◽  
Maria Pizzichini ◽  
Daniela Vannoni ◽  
Antonella Tabucchi ◽  
...  
Keyword(s):  
Rat Liver ◽  
Threonine Deaminase

Restoration of rat liver L-threonine deaminase by pyridoxamine 5′-phosphate

1992 ◽  
Vol 20 (1) ◽  
pp. 35S-35S ◽  
Author(s):  
E. MARINELLO ◽  
R. LEONCINI ◽  
R. GUERRANTI ◽  
S. RIGHI ◽  
R. PAGANI
Keyword(s):  
Rat Liver ◽  
Threonine Deaminase

In vitro Regulation of Rat Liver L-Threonine Deaminase by Different Effectors

Enzyme ◽  
1990 ◽  
Vol 43 (3) ◽  
pp. 122-128 ◽  
Author(s):  
Roberto Pagani ◽  
Roberto Leoncini ◽  
Lucia Terzuoli ◽  
Roberto Guerranti ◽  
Enrico Marinello
Keyword(s):  
Rat Liver ◽  
Threonine Deaminase

Rat liver L-threonine deaminase: Properties and purification

1985 ◽  
Vol 5 (6) ◽  
pp. 499-508 ◽  
Author(s):  
R. Leoncini ◽  
R. Pagani ◽  
A. Casella ◽  
E. Marinello
Keyword(s):  
Thermal Stability ◽  
Rat Liver ◽  
Competitive Inhibitor ◽  
New Method ◽  
Optimum Temperature ◽  
Temperature Optimum ◽  
Threonine Deaminase ◽  
Ph Optimum ◽  
Carbonate Ions

A new method of purification of rat liver L-threonine deaminase has been developed, and the results obtained are compared with values obtained by other authors. Some properties of this enzyme (pH optimum, temperature optimum, thermal stability, specificity, etc.) have been examined and we found that the enzyme is inhibited by carbonate ions, that L-cysteine (a competitive inhibitor) is also an inactivator of the enzyme and that it is bound to the enzyme in a ratio of 0.25 mole of cysteine per mole of enzyme, supporting the hypothesis that the enzyme consists of 4 subunits.

Regulation of acetyl-CoA carboxylase by glucagon in HeLa cells

1985 ◽  
Vol 5 (6) ◽  
pp. 491-497
Author(s):  
R. P. Bhullar ◽  
K. Dakshinamurti
Keyword(s):  
Thermal Stability ◽  
Rat Liver ◽  
Hela Cells ◽  
Competitive Inhibitor ◽  
Acetyl Coa Carboxylase ◽  
Optimum Temperature ◽  
Temperature Optimum ◽  
Threonine Deaminase ◽  
Ph Optimum ◽  
Carbonate Ions

A new method of purification of rat liver L-threonine deaminase has been developed, and the results obtained are compared with values obtained by other authors. Some properties of this enzyme (pH optimum, temperature optimum, thermal stability, specificity, etc.) have been examined and we found that the enzyme is inhibited by carbonate ions, that L-cysteine (a competitive inhibitor) is also an inactivator of the enzyme and that it is bound to the enzyme in a ratio of 0.25 mole of cysteine per mole of enzyme, supporting the hypothesis that the enzyme consists of 4 subunits.

Structure and function correlations between the rat liver threonine deaminase and aminotransferases

2003 ◽  
Vol 1645 (1) ◽  
pp. 40-48 ◽  
Author(s):  
Maria Scarselli ◽  
Maria Giuseppina Padula ◽  
Andrea Bernini ◽  
Ottavia Spiga ◽  
Arianna Ciutti ◽  
...  
Keyword(s):  
Rat Liver ◽  
Structure And Function ◽  
Threonine Deaminase ◽  
And Function

An improved method for purification of l-threonine deaminase from rat liver

1990 ◽  
Vol 20 (2) ◽  
pp. 97-105 ◽  
Author(s):  
R. Leoncini ◽  
R. Guerranti ◽  
R. Pagani ◽  
E. Marinello
Keyword(s):  
Rat Liver ◽  
Improved Method ◽  
Threonine Deaminase

Initial Polymerization Sites Indicated During Mitochondrial Oxidation of Diaminobenzidine after Toluene Treatment

1977 ◽  
Vol 35 ◽  
pp. 408-409
Author(s):  
W. A. Shannon ◽  
M. A. Matlib
Keyword(s):  
Membrane Permeability ◽  
Cytochrome Oxidase ◽  
Rat Liver ◽  
Precise Definition ◽  
Cytochemical Localization ◽  
Oxidative Reaction ◽  
Mitochondrial Oxidation ◽  
Definition Of ◽  
Exogenous Substrates

Numerous studies have dealt with the cytochemical localization of cytochrome oxidase via cytochrome c. More recent studies have dealt with indicating initial foci of this reaction by altering incubation pH (1) or postosmication procedure (2,3). The following study is an attempt to locate such foci by altering membrane permeability. It is thought that such alterations within the limits of maintaining morphological integrity of the membranes will ease the entry of exogenous substrates resulting in a much quicker oxidation and subsequently a more precise definition of the oxidative reaction.The diaminobenzidine (DAB) method of Seligman et al. (4) was used. Minced pieces of rat liver were incubated for 1 hr following toluene treatment (5,6). Experimental variations consisted of incubating fixed or unfixed tissues treated with toluene and unfixed tissues treated with toluene and subsequently fixed.

Effects of 5-5'-Diphenyl-2-thiohydantoin (DPTH) and Thyroxine on the Ultrastructure and Chemical Composition of Rat Liver

1971 ◽  
Vol 29 ◽  
pp. 570-571
Author(s):  
E. A. Elfont ◽  
R. B. Tobin ◽  
D. G. Colton ◽  
M. A. Mehlman
Keyword(s):  
Chemical Composition ◽  
Rat Liver ◽  
Future Study ◽  
Mode Of Action ◽  
Liver Mitochondria ◽  
Rat Liver Mitochondria ◽  
Effective Inhibitor ◽  
Biochemical Effects ◽  
Glycerophosphate Dehydrogenase ◽  
Stimulation Of

Summary5,-5'-diphenyl-2-thiohydantoin (DPTH) is an effective inhibitor of thyroxine (T4) stimulation of α-glycerophosphate dehydrogenase in rat liver mitochondria. Because this finding indicated a possible tool for future study of the mode of action of thyroxine, the ultrastructural and biochemical effects of DPTH and/or thyroxine on rat liver mere investigated.Rats were fed either standard or DPTH (0.06%) diet for 30 days before T4 (250 ug/kg/day) was injected. Injection of T4 occurred daily for 10 days prior to sacrifice. After removal of the liver and kidneys, part of the tissue was frozen at -50°C for later biocheailcal analyses, while the rest was prefixed in buffered 3.5X glutaraldehyde (390 mOs) and post-fixed in buffered 1Z OsO4 (376 mOs). Tissues were embedded in Araldlte 502 and the sections examined in a Zeiss EM 9S.Hepatocytes from hyperthyroid rats (Fig. 2) demonstrated enlarged and more numerous mitochondria than those of controls (Fig. 1). Glycogen was almost totally absent from the cytoplasm of the T4-treated rats.

Effects of Steroids on Fetal Rat Liver

1969 ◽  
Vol 27 ◽  
pp. 350-351
Author(s):  
F. G. Zaki
Keyword(s):  
Liver Injury ◽  
Rat Liver ◽  
Fetal Liver ◽  
Dosage Level ◽  
Maternal Plasma ◽  
Methyl Prednisolone ◽  
Fetal Rat ◽  
Toxic Agents ◽  
Fetal Rat Liver ◽  
Neonatal Liver

Fetal and neonatal liver injury induced by agents circulating in maternal plasma, even though well recognized, its morphological manifestations are not yet established. As part of our studies of fetal and neonatal liver injury induced by maternal nutritional disorders, metabolic impairment and toxic agents, the effects of two anti-inflammatory steroids have been recently inves tigated.Triamcinolone and methyl prednisolone were injected each in a group of rats during pregnancy at a-dosage level of 2 mgm three times a week. Fetal liver was studied at 18 days of gestation. Litter size and weight markedly decreased than those of control rats. Stillbirths and resorption were of higher incidence in the triamcinolone group than in those given the prednisolone.

Effects of Hypophysectomy on the Fine Structure of Rat Liver Cells

1967 ◽  
Vol 25 ◽  
pp. 156-157
Author(s):  
Robert R. Cardell
Keyword(s):  
Electron Microscopy ◽  
Fine Structure ◽  
Rat Liver ◽  
Liver Cell ◽  
Anterior Pituitary ◽  
Liver Cells ◽  
Biochemical Studies ◽  
Liver Functions ◽  
Rat Liver Cells ◽  
And Control

Hypophysectomy of the rat renders this animal deficient in the hormones of the anterior pituitary gland, thus causing many primary and secondary hormonal effects on basic liver functions. Biochemical studies of these alterations in the rat liver cell are quite extensive; however, relatively few morphological observations on such cells have been recorded. Because the available biochemical information was derived mostly from disrupted and fractionated liver cells, it seemed desirable to examine the problem with the techniques of electron microscopy in order to see what changes are apparent in the intact liver cell after hypophysectomy. Accordingly, liver cells from rats which had been hypophysectomized 5-120 days before sacrifice were studied. Sham-operated rats served as controls and both hypophysectomized and control rats were fasted 15 hours before sacrifice.

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