scholarly journals Enzyme histochemistry of developing rat oral mucosa.

1981 ◽  
Vol 29 (1) ◽  
pp. 57-64 ◽  
Author(s):  
S Sjögren ◽  
L Hammarström ◽  
A Larsson
Keyword(s):  
Alkaline Phosphatase ◽  
Acid Phosphatase ◽  
Lactate Dehydrogenase ◽  
Succinate Dehydrogenase ◽  
Oral Mucosa ◽  
Adenosine Triphosphatase ◽  
Enzyme Histochemistry ◽  
Glucose 6 Phosphate Dehydrogenase ◽  
Developing Rat

The oral mucosa of developing and mature rats was analyzed histochemically for regional enzyme differences. The following enzymes were studied: nonspecific alkaline phosphatase (alkpase), acid phosphatase (acidpase), 5'-nucleotidase (AMPase), adenosine triphosphatase (ATPase), succinate dehydrogenase (SDH), lactate dehydrogenase (LDH), and glucose-6-phosphate dehydrogenase (G-6-pDH). All enzymes were active in the oral mucosa, but regional as well as tissue variations were observed. Epithelium in all regions showed acidpase staining. Oxidoreductases were found in all regions with variations within the epithelium. The epithelium of specific regions stained for alkpase and AMPase, while adjacent epithelium did not. We suggest that the alkpase and AMPase activities are associated with specific functions of the epithelium in these regions.

scholarly journals CYTOCHEMISTRY AND ELECTRON MICROSCOPY

1963 ◽  
Vol 17 (1) ◽  
pp. 19-58 ◽  
Author(s):  
David D. Sabatini ◽  
Klaus Bensch ◽  
Russell J. Barrnett
Keyword(s):  
Electron Microscopy ◽  
Alkaline Phosphatase ◽  
Fine Structure ◽  
Acid Phosphatase ◽  
Adenosine Triphosphatase ◽  
Osmium Tetroxide ◽  
Enzyme Histochemistry ◽  
Succinic Dehydrogenase ◽  
Optimal Conditions ◽  
Fixation Procedure

The aldehydes introduced in this paper and the more appropriate concentrations for their general use as fixatives are: 4 to 6.5 per cent glutaraldehyde, 4 per cent glyoxal, 12.5 per cent hydroxyadipaldehyde, 10 per cent crotonaldehyde, 5 per cent pyruvic aldehyde, 10 per cent acetaldehyde, and 5 per cent methacrolein. These were prepared as cacodylate- or phosphate-buffered solutions (0.1 to 0.2 M, pH 6.5 to 7.6) that, with the exception of glutaraldehyde, contained sucrose (0.22 to 0.55 M). After fixation of from 0.5 hour to 24 hours, the blocks were stored in cold (4°C) buffer (0.1 M) plus sucrose (0.22 M). This material was used for enzyme histochemistry, for electron microscopy (both with and without a second fixation with 1 or 2 per cent osmium tetroxide) after Epon embedding, and for the combination of the two techniques. After fixation in aldehyde, membranous differentiations of the cell were not apparent and the nuclear structure differed from that commonly observed with osmium tetroxide. A postfixation in osmium tetroxide, even after long periods of storage, developed an image that—notable in the case of glutaraldehyde—was largely indistinguishable from that of tissues fixed under optimal conditions with osmium tetroxide alone. Aliesterase, acetylcholinesterase, alkaline phosphatase, acid phosphatase, 5-nucleotidase, adenosine triphosphatase, and DPNH and TPNH diaphorase activities were demonstrable histochemically after most of the fixatives. Cytochrome oxidase, succinic dehydrogenase, and glucose-6-phosphatase were retained after hydroxyaldipaldehyde and, to a lesser extent, after glyoxal fixation. The final product of the activity of several of the above-mentioned enzymes was localized in relation to the fine structure. For this purpose the double fixation procedure was used, selecting in each case the appropriate aldehyde.

scholarly journals Studies of the Distribution and Source of Enzymes in Mammalian Semen

1968 ◽  
Vol 21 (3) ◽  
pp. 483 ◽  
Author(s):  
RN Murdoch ◽  
IG White
Keyword(s):  
Alkaline Phosphatase ◽  
Lactate Dehydrogenase ◽  
Succinate Dehydrogenase ◽  
Human Semen ◽  
Acid And Alkaline Phosphatase ◽  
Glucose 6 Phosphate Dehydrogenase

Succinate dehydrogenase (SDH), lactate dehydrogenase (LDH), glutamateoxaloacetate transaminase (GOT), and acid and alkaline phosphatase are present in ram, bull, dog, rabbit, and human semen but the concentrations differ from one species to another. Amylase is found in the semen of all these species except the ram, and glucose�6-phosphate dehydrogenase (GDH) in all except the bull.

Comparison of human and murine isolates of Schistosoma mansoni from Richard-Toll, Senegal, by isoelectric focusing

1997 ◽  
Vol 71 (2) ◽  
pp. 175-181 ◽  
Author(s):  
M. Sène ◽  
P. Brémond ◽  
J.P. Hervé ◽  
V.R. Southgate ◽  
B. Sellin ◽  
...  
Keyword(s):  
Genetic Variation ◽  
Acid Phosphatase ◽  
Lactate Dehydrogenase ◽  
Schistosoma Mansoni ◽  
Isoelectric Focusing ◽  
Glucose Phosphate Isomerase ◽  
Glucose Phosphate ◽  
Enzyme Systems ◽  
Glucose 6 Phosphate Dehydrogenase ◽  
Arvicanthis Niloticus

AbstractStudies on human and murine isolates of Schistosoma mansoni, from Richard-Toll, Senegal, were carried out by isoelectric focusing in polyacrylamide gels. Seven enzyme systems; lactate dehydrogenase (LDH), malate dehydrogenase (MDH), glucose-6-phosphate dehydrogenase (G6PD), acid phosphatase (AcP), hexokinase (HK), glucose phosphate isomerase (GPI), and phosphoglucomutase (PGM), were used to compare the two isolates. All systems tested, apart from LDH, were found to be polymorphic for both isolates. Interestingly, one phenotype is more frequent than the remainder. The results show that there is no significant genetic variation between the S. mansoni isolates from man and the rodents, Arvicanthis niloticus and Mastomys huberti.

Histochemical studies on Raillietina (Raillietina) johri (Cestoda: Davaineidae). I. Nonspecific and specific phosphatases

1979 ◽  
Vol 53 (1) ◽  
pp. 45-49 ◽  
Author(s):  
T. K. Roy
Keyword(s):  
Alkaline Phosphatase ◽  
Acid Phosphatase ◽  
Atpase Activity ◽  
Functional Significance ◽  
Adenosine Triphosphatase ◽  
Vas Deferens ◽  
Gland Cells ◽  
Vitelline Gland ◽  
Receptaculum Seminis ◽  
Almost All

ABSTRACTCertain phosphatases have been localized by histochemical techniques in various tissues of a pigeon cestode, Raillietina (Raillietina) johri. Acid phosphatase (AcPase), alkaline phosphatase (AlPase) and adenosine triphosphatase (ATPase) were present in almost all structures: tegument; subtegumental muscles; subtegumental cells; excretory canal; tsetes; sperm ductules; vas deferens; cirrus sac; cirrus; ovary; receptaculum seminis; vagina; vitelline gland cells; oocytes; uterus; embryonated eggs. AlPase was absent in parenchyma, spermatocytes, spermatids and spermatozoa. AlPase activity was more intense in the tegument of mature gravid proglottides. AcPase and ATPase were visualized in various stages of spermatogenesis of the parasite. ATPase activity was also observed in chromosomes. 5'-nucleotidase (AMPase) activity was restricted to embryonated eggs only. Functional significance of these phosphatases is discussed.

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.

scholarly journals LEUKEMIA EVOKED WITH 7, 8, 12-TRIMETHYLBENZ(A)ANTHRACENE IN RAT

1971 ◽  
Vol 134 (5) ◽  
pp. 1285-1297 ◽  
Author(s):  
Colin Bird ◽  
Charles Huggins
Keyword(s):  
Stem Cells ◽  
Alkaline Phosphatase ◽  
Acid Phosphatase ◽  
Lactate Dehydrogenase ◽  
Subsequent Development ◽  
Nodule Formation ◽  
Leukemic Stem Cells ◽  
Immature Rats ◽  
Enzyme Changes ◽  
Red Pulp

An early sign of erythroblastic leukemia in rat was nodule formation in the spleen. Hyperplastic foci of stem cells, indistinguishable histologically from leukemic stem cells, were found in the red pulp whereas the malpighian corpuscles were uninvolved. Anemia is a normal phenomenon in immature rats and the spleen of the prepubertal rat possesses considerable hemopoietic potential. Pulse-doses of 7, 8, 12-trimethylbenz(a)anthracene prevented the physiologic hematological development of maturing rats and was associated with subsequent development of leukemic stem cells in the red pulp of the spleen. Significant enzyme changes were observed in leukemic spleens. Compared with the spleens of normal littermates, the concentration of lactate dehydrogenase rose while that of malate dehydrogenase fell; the content of alkaline phosphatase rose whereas acid phosphatase fell. Increased alkaline phosphatase activity in leukemic spleen was attributed to nonleukemic foci of myelopoiesis.

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