THE ACTIVITY OF ENZYMES IN THE RABBIT UTERUS AND EFFECT OF PROGESTERONE AND OESTRADIOL

1969 ◽  
Vol 43 (2) ◽  
pp. 167-174 ◽  
Author(s):  
R. N. MURDOCH ◽  
I. G. WHITE
Keyword(s):  
Alkaline Phosphatase ◽  
Enzyme Activity ◽  
Succinic Dehydrogenase ◽  
Lactic Dehydrogenase ◽  
Glutamate Oxaloacetate Transaminase ◽  
Oestrogen Treatment ◽  
Uterine Endometrium ◽  
Uterine Fluid ◽  
Activity Of Enzymes ◽  
Glucose 6 Phosphate Dehydrogenase

SUMMARY The activity of several enzymes has been measured in the uterine endometrium of the rabbit during oestrus and pseudopregnancy and after injecting oestradiol benzoate or progesterone 28 days after ovariectomy. The enzyme activity of the uterine fluid has been determined during oestrus and the effect of uterine ligation studied. Progesterone and the induction of pseudopregnancy stimulated succinic dehydrogenase (SDH) and glucose-6-phosphate dehydrogenase (GDH) activity and depressed amylase and lactic dehydrogenase (LDH) activity. In ovariectomized does, glutamate-oxaloacetate transaminase (GOT) activity increased after the injection of progesterone. Progesterone also stimulated endometrial phosphatase after ovariectomy but, when given after a period of oestrogen treatment, it limited the even greater response of acid and alkaline phosphatase to oestrogen; the activity then attaining the same level as when progesterone alone was given. SDH, GDH and glycerylphosphorylcholine (GPC) diesterase could not be detected in uterine fluid but amylase and alkaline phosphatase were in greater concentration than in the endometrium. GPC diesterase was, however, found to be present in uterine tissue. Ligation of the uterus did not significantly alter the enzyme activity of the endometrium.

Identification and regulation of the platelet-activating factor acetylhydrolase activity in the mouse uterus in early pregnancy

2001 ◽  
Vol 13 (6) ◽  
pp. 367 ◽  
Author(s):  
O. Chami ◽  
C. O'Neill
Keyword(s):  
Enzyme Activity ◽  
Early Pregnancy ◽  
Platelet Activating Factor ◽  
Density Lipoprotein ◽  
Mouse Uterus ◽  
Uterine Endometrium ◽  
Native Molecular Mass ◽  
Platelet Activating Factor Acetylhydrolase ◽  
Uterine Fluid ◽  
Detergent Treatment

Platelet-activating factor (PAF) is a product of the embryo and the endometrium in early pregnancy. The actions of PAF may be regulated by its degradation and this is largely achieved by the enzyme PAF acetylhydrolase (PAF:ah; EC 3.1.1.47). The present study characterized the PAF:ah in the endometrium and uterine fluid of mice during early pregnancy. The enzyme activity from uterine endometrium and luminal fluids had the same biochemical characteristics as the plasma form of the enzyme. The three sources of enzyme activity (i) had an apparent native molecular mass greater than 106 Da, but this was reduced after detergent treatment and purification to 60–65 kDa; (ii) bound to cholesterol hemisuccinate agarose matrix; and (iii) were found in the high density lipoprotein-enriched fraction after density gradient ultracentrifugation. In castrate females, oestradiol-17β (E2) caused a dose-dependent increase in the activity of the enzyme in endometrium and luminal fluid. Progesterone (P4) inhibited the E2-induced increase in PAF:ah in uterine tissue. Treatment with E2 alone caused an increase in endometrial PAF:ah activity within 24 h, which declined within 48 h. In luminal fluid, the same treatment caused increased activity within 24 h, peaking after 48 h of treatment and then declining. In E2-treated castrate females, mRNA for an intracellular (but not plasma) form of PAF:ah was detected, yet the intracellular form was not detected biochemically. The results suggest that most of the enzyme activity was not produced locally, but probably resulted from the influx of the plasma form of the enzyme.

THE METABOLISM OF THE ERYTHROCYTE: XIII. ENZYME ACTIVITY IN THE RETICULOCYTE

1956 ◽  
Vol 34 (2) ◽  
pp. 222-235 ◽  
Author(s):  
D. Rubinstein ◽  
P. Ottolenghi ◽  
O. F. Denstedt
Keyword(s):  
Enzyme Activity ◽  
Cytochrome Oxidase ◽  
Reticulocyte Count ◽  
Soluble Fraction ◽  
Succinic Dehydrogenase ◽  
Insoluble Fraction ◽  
Severe Anemia ◽  
Subcutaneous Injections ◽  
Blood Specimens ◽  
Glucose 6 Phosphate Dehydrogenase

The object of the study was to ascertain the changes that occur in the activity of the enzymes of the reticulocyte during its maturation to the normocyte (adult erythrocyte). Blood specimens were taken from rabbits in which a severe anemia and a pronounced reticulosis (50–90% reticulocyte count) had been produced by giving the animals subcutaneous injections of acetylphenylhydrazine. Succinic dehydrogenase, cytochrome oxidase, and DPN-ase were found to be confined to the insoluble fraction of the cells while glucose-6-phosphate dehydrogenase and pyrophosphatase were found only in the soluble fraction (stroma-free hemolyzate). Isocitric, lactic, and malic dehydrogenases, fumarase, aconitase, and hexokinase were found to be present in both fractions. The activity of fumarase, hexokinase, and pyrophosphatase is much lower in the normocyte than in the reticulocyte while that of the isocitric, lactic, and malic dehydrogenases and of DPN-ase was of the same order in both types of cell. Aliquots of blood specimens were kept at 37 °C. for 12 hr. and the activity of numerous enzymes was followed at two-hourly intervals. The enzymes which are more active in the reticulocyte undergo a diminution in activity concurrently with the decrease in the reticulocyte count. Succinic dehydrogenase, cytochrome oxidase, and aconitase are absent from the normocyte. The significance of these changes with respect to the maturation of the reticulocyte is discussed.Exposure of hemolyzates of the blood specimens to the enzyme ribonuclease, to destroy any ribonucleic acid that may be present, did not alter the activity of any of the enzymes tested. The DPN-ase of the reticulocyte, as in the normocyte, was found to be a nucleosidase which splits the linkage between nicotinamide and ribose.

A Histological and Histochemical Study of the Brown and Yellow Adipose Tissue of the Bat, Hipposideros speoris

1959 ◽  
Vol s3-100 (51) ◽  
pp. 369-375
Author(s):  
J. C. GEORGE ◽  
J. EAPEN
Keyword(s):  
Alkaline Phosphatase ◽  
Adipose Tissue ◽  
Acid Phosphatase ◽  
Adenosine Triphosphatase ◽  
Succinic Dehydrogenase ◽  
Lactic Dehydrogenase ◽  
Histological Structure ◽  
Brown Adipose ◽  
Aldehydes And Ketones ◽  
Sulphydryl Groups

A study of the histology and histochemical reactions for lipase, alkaline phosphatase, acid phosphatase, adenosine triphosphatase, succinic dehydrogenase, lactic dehydrogenase, phospholipids, cholesterol, sulphydryl groups, and water-insoluble aldehydes and ketones in the brown and yellow adipose tissue of the bat (Hipposideros speoris) revealed that the two types of adipose tissue differ in histological structure as well as physiological activity. The histological structure of the two types of adipose tissue was found to be different, resembling that of the two corresponding types of the rat. The brown adipose tissue showed a higher concentration of succinic dehydrogenase, lactic dehydrogenase, phospholipids, cholesterol, and sulphydryl groups. No detectable difference between brown and yellow adipose tissue was, however, found with respect to lipase, alkaline phosphatase, acid phosphatase, adenosine triphosphatase, and water-insoluble aldehydes and ketones.

Early changes in serum enzymes in the rat following burn trauma

1963 ◽  
Vol 18 (4) ◽  
pp. 818-820 ◽  
Author(s):  
Arthur A. Spector ◽  
Wayne A. Pauli
Keyword(s):  
Leucine Aminopeptidase ◽  
Burn Injury ◽  
Chemical Constituents ◽  
Succinic Dehydrogenase ◽  
Lactic Dehydrogenase ◽  
Active Protein ◽  
Adult Rats ◽  
Ether Anesthesia ◽  
Glucose 6 Phosphate Dehydrogenase

Under ether anesthesia, 30% surface area scalds were administered to young adult rats. Controls were treated similarly except for the scald. The animals were sacrificed at 15 min after injury, and their serum was analyzed for enzyme activities and chemical constituents. Large increases in catalase, glucose 6-phosphate dehydrogenase, lactic dehydrogenase, glutamic-oxalacetic transaminase, and glutamic-pyruvic transaminase activites were noted in postburn serum. No statistically significant change was found in acetylcholinesterase, acid phosphatase, alkaline phosphatase, leucine aminopeptidase, 5'-nucleotidase, or succinic dehydrogenase. Amylase activity was decreased in the burned animals. Serum oxyhemoglobin and inorganic phosphate were elevated, but total protein remained unchanged following trauma. The etiology of the early postburn serum changes is believed to be tissue damage produced by the burn, an important component of which is in vivo hemolysis. A possible relationship between the rapid extracellular buildup of enzymatically active protein and the pathology of burn injury is suggested. Submitted on November 15, 1962

scholarly journals ENZYMATIC AND CHROMOSOMAL CHARACTERIZATION OF HELA VARIANTS

1969 ◽  
Vol 41 (3) ◽  
pp. 806-815 ◽  
Author(s):  
R. H. Bottomley ◽  
A. L. Trainer ◽  
M. J. Griffin
Keyword(s):  
Alkaline Phosphatase ◽  
Chromosome Number ◽  
Cell Line ◽  
Lactic Dehydrogenase ◽  
Single Chromosome ◽  
Modal Chromosome Number ◽  
Cell Strains ◽  
Hela S3 ◽  
Glucose 6 Phosphate Dehydrogenase

Seven strains of HeLa cells have been characterized by the number of chromosomes and the activity of the enzymes alkaline phosphatase, glucose-6-phosphate dehydrogenase, 6-phosphogluconic dehydrogenase, and lactic dehydrogenase. All seven strains were found to differ as to chromosome numbers and enzyme levels despite the fact that two strains were called HeLa and three were called HeLa S3. Three strains were found to have a stemline in which greater than 60% of the cells demonstrated a single chromosome number, and this characteristic was stable for at least 6 months. A nomenclature for these clones has been suggested by the use of the stemline chromosome number as a subscript following HeLa. These three clones were, therefore, designated HeLa65, HeLa71, and HeLa75. Karyotypes were made of the stemlines of these clones and were compared with enzyme levels. Alkaline phosphatase showed the greatest variation from cell line to cell line with a 200-fold difference in levels, whereas glucose-6-phosphate dehydrogenase showed variation in activity over a 12-fold range, lactic dehydrogenase over an 8-fold range, and 6-phosphogluconic dehydrogenase over a 2-fold range. It is suggested that human cell strains can be used for biochemical studies if they are cloned and if the clones are relatively stable at least with respect to modal chromosome number and karyotype.

Evaluation of Buffalo Colostrum Quality by Estimation of Enzyme Activity Levels

2001 ◽  
Vol 64 (8) ◽  
pp. 1265-1267 ◽  
Author(s):  
P. LOMBARDI ◽  
L. AVALLONE ◽  
U. PAGNINI ◽  
D. d'ANGELO ◽  
E. BOGIN
Keyword(s):  
Alkaline Phosphatase ◽  
Enzyme Activity ◽  
Gamma Globulin ◽  
Correlation Coefficients ◽  
Lactic Dehydrogenase ◽  
General Linear Model ◽  
Activity Levels ◽  
Electrophoretic Separation ◽  
General Linear Model Procedure ◽  
Potential Use

A study to evaluate the value and potential use of colostral enzymes as markers for the evaluation of buffalo colostrum quality was conducted. The enzymes γ-glutamyltransferase (GGT), lactic dehydrogenase (LDH), and alkaline phosphatase (ALP) in buffalo's colostrum were measured spectrophotometrically, and their activities were correlated with the gamma-globulin content. Gamma-globulin concentration was determined following the electrophoretic separation of the colostral proteins and quantified with a densitometer. Colostrum was obtained from 15 dams, soon after calving. Means, standard deviations, correlation coefficients, and degree of significance were calculated using the general linear model procedure of the Statistical Analysis Systems program. The activity of GGT in the colostrum was the highest, followed by LDH and ALP. A significant correlation (r = 0.86; P < 0.001) was seen between GGT and gamma-globulin concentration in the colostrum, supporting the suggestion of using this enzyme as a marker for the evaluation of colostrum quality.

Histoenzymic distribution of phosphatases, dehydrogenases and esterasesin ileal peyer’s patches of neonatal buffalo calves

2017 ◽  
Author(s):  
Kritima Kapoor
Keyword(s):  
Lactic Dehydrogenase ◽  
Peripheral Region ◽  
Peyer's Patches ◽  
Peyer’S Patches ◽  
Buffalo Calves ◽  
Strong Activity ◽  
Lymphoid Follicles ◽  
Dehydrogenase Enzyme ◽  
Activity Of Enzymes ◽  
Glucose 6 Phosphate Dehydrogenase

The histoenzymic study was conducted on ileum of neonatal buffalo calves (n=15) and their age was estimated by observing their temporary and permanent dentition. Histoenzymic distribution of different enzymes was studied on ileal peyer’s patches of neonatal buffalo calves. Strong activity of AKPase was observed at the dome and capsule of the peyer’s patch lymphoid follicles at this age. However, moderate Lactic dehydrogenase (LDH) and SDH activity was observed within the ileal lymphoid follicles. A strong activity of Glucose-6-phosphate dehydrogenase enzyme was observed in the follicles at their periphery and within center of few follicles. Also a strong positive activity of diaphorases was observed in peripheral region of the follicle as fine granular reaction. The activity of enzymes has been discussed with the physiological function of the tissue..

scholarly journals The Demonstration of Dehydrogenases and Diaphorases in Cells of Peripheral Blood and Bone Marrow

Blood ◽  
1967 ◽  
Vol 29 (5) ◽  
pp. 737-746 ◽  
Author(s):  
L. ROZENSZAJN ◽  
DAVIDIA SHOHAM
Keyword(s):  
Bone Marrow ◽  
Enzymatic Activity ◽  
Bone Marrow Cells ◽  
White Blood Cells ◽  
Succinic Dehydrogenase ◽  
Lactic Dehydrogenase ◽  
Enzymatic Action ◽  
Specific Enzymatic Activity ◽  
Glucose 6 Phosphate Dehydrogenase ◽  
In Cells

Abstract Nicotinamide adenine dinucleotide-linked dehydrogenases, SDH, NADH and NADPH diaphorases were assayed with cytochemical methods in white blood cells in bone marrow cells using tetrazolium salts, Nitro-BT and MTT. In unfixed smears specific enzymatic activity was demonstrated for glucose-6-phosphate dehydrogenase, succinic dehydrogenase and NADH diaphorase. In fixed smears the activity of lactic dehydrogenase and succinic dehydrogenase was shown. The action of NADH and NADPH diaphorases was demonstrated in the fixed smears only in the presence of NADH and NADPH. Supravital methods are inadequate for demonstration of specific enzymatic activity. Lactic dehydrogenase activity in cells was estimated in a semiquantitative way. The enzymatic action of the dehydrogenases and the diaphorases was stronger in younger cells and decreased progressively with their maturation.

scholarly journals Lymphocyte and Granulocyte Enzyme Activity in Patients with Down’s Syndrome

Blood ◽  
1967 ◽  
Vol 30 (5) ◽  
pp. 669-673 ◽  
Author(s):  
HENRY L. NADLER ◽  
PATRICIA L. MONTELEONE ◽  
TOHRU INOUYE ◽  
DAVID YI-YUNG HSIA
Keyword(s):  
Alkaline Phosphatase ◽  
Enzyme Activity ◽  
Acid Phosphatase ◽  
Blood Cells ◽  
Polymorphonuclear Leukocytes ◽  
White Blood Cells ◽  
Down's Syndrome ◽  
Down’S Syndrome ◽  
Glucose 6 Phosphate Dehydrogenase ◽  
Phosphatase Alkaline

Abstract Patients with trisomic Down’s syndrome were found to have significant increases of acid phosphatase, alkaline phosphatase, and glucose-6-phosphate dehydrogenase in both lymphocytes and polymorphonuclear leukocytes separated from white blood cells by the procedure of Rabinowitz. The alteration in enzyme activities appears not to be directly related to genes located on the chromosome causing Down’s syndrome.

THE METABOLISM OF THE ERYTHROCYTE: XIII. ENZYME ACTIVITY IN THE RETICULOCYTE

1956 ◽  
Vol 34 (1) ◽  
pp. 222-235 ◽  
Author(s):  
D. Rubinstein ◽  
P. Ottolenghi ◽  
O. F. Denstedt
Keyword(s):  
Enzyme Activity ◽  
Cytochrome Oxidase ◽  
Reticulocyte Count ◽  
Soluble Fraction ◽  
Succinic Dehydrogenase ◽  
Insoluble Fraction ◽  
Severe Anemia ◽  
Subcutaneous Injections ◽  
Blood Specimens ◽  
Glucose 6 Phosphate Dehydrogenase

The object of the study was to ascertain the changes that occur in the activity of the enzymes of the reticulocyte during its maturation to the normocyte (adult erythrocyte). Blood specimens were taken from rabbits in which a severe anemia and a pronounced reticulosis (50–90% reticulocyte count) had been produced by giving the animals subcutaneous injections of acetylphenylhydrazine. Succinic dehydrogenase, cytochrome oxidase, and DPN-ase were found to be confined to the insoluble fraction of the cells while glucose-6-phosphate dehydrogenase and pyrophosphatase were found only in the soluble fraction (stroma-free hemolyzate). Isocitric, lactic, and malic dehydrogenases, fumarase, aconitase, and hexokinase were found to be present in both fractions. The activity of fumarase, hexokinase, and pyrophosphatase is much lower in the normocyte than in the reticulocyte while that of the isocitric, lactic, and malic dehydrogenases and of DPN-ase was of the same order in both types of cell. Aliquots of blood specimens were kept at 37 °C. for 12 hr. and the activity of numerous enzymes was followed at two-hourly intervals. The enzymes which are more active in the reticulocyte undergo a diminution in activity concurrently with the decrease in the reticulocyte count. Succinic dehydrogenase, cytochrome oxidase, and aconitase are absent from the normocyte. The significance of these changes with respect to the maturation of the reticulocyte is discussed.Exposure of hemolyzates of the blood specimens to the enzyme ribonuclease, to destroy any ribonucleic acid that may be present, did not alter the activity of any of the enzymes tested. The DPN-ase of the reticulocyte, as in the normocyte, was found to be a nucleosidase which splits the linkage between nicotinamide and ribose.

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