Intestinal leucine aminopeptidase and alkaline phosphatase: Genetic regulation and development in mice

1990 ◽  
Vol 28 (5-6) ◽  
pp. 267-281 ◽  
Author(s):  
Mary-Fleming Finlay ◽  
Laryssa McCloud
Keyword(s):  
Alkaline Phosphatase ◽  
Leucine Aminopeptidase ◽  
Genetic Regulation

Serum Gamma-Glutamyl Transpeptidase Activity as an Indicator of Disease of Liver, Pancreas, or Bone

1972 ◽  
Vol 18 (4) ◽  
pp. 358-362 ◽  
Author(s):  
Gifford Lum ◽  
S Raymond Gambino
Keyword(s):  
Alkaline Phosphatase ◽  
Liver Disease ◽  
Viral Hepatitis ◽  
Bone Disease ◽  
Leucine Aminopeptidase ◽  
Serum Alkaline Phosphatase ◽  
Metastatic Carcinoma ◽  
Gamma Glutamyl Transpeptidase ◽  
Serum Alkaline Phosphatase Activity ◽  
Glutamyl Transpeptidase

Abstract Serum γ-glutamyl transpeptidase (GGT), leucine aminopeptidase, alkaline phosphatase, alanine aminotransferase, and aspartate aminotransferase activities were assayed in controls and in patients with liver, pancreatic, or bone disease. GGT activity was above normal in all forms of liver disease studied (viral hepatitis, cirrhosis, cholecystitis, metastatic carcinoma to liver, pancreatic carcinoma, liver granuloma, and acute pancreatitis). GGT more sensitively indicated hepatic disease than did alkaline phosphatase, much more so than did leucine aminopeptidase. GGT was disproportionately more active in relation to the transaminases in cases of intraor extrahepatic biliary obstruction; the reverse was true in cases of viral hepatitis. GGT activity was normal in children, adolescents, and pregnant women, and in cases of bone disease and renal failure. Kinetic measurement of GGT activity offers a simple, sensitive, and direct means for distinguishing whether bone or liver is the source of increased serum alkaline phosphatase activity. Activity was highest in obstructive liver disease.

Na+/H+ antiporter in membrane populations resolved from a renal brush border vesicle preparation

1984 ◽  
Vol 246 (6) ◽  
pp. F853-F858
Author(s):  
A. K. Mircheff ◽  
H. E. Ives ◽  
V. J. Yee ◽  
D. G. Warnock
Keyword(s):  
Alkaline Phosphatase ◽  
Cytochrome C ◽  
Brush Border ◽  
Brush Border Membrane ◽  
Leucine Aminopeptidase ◽  
Membrane Preparation ◽  
Phase System ◽  
Cytochrome C Reductase ◽  
Nadph Cytochrome ◽  
Nadph Cytochrome C Reductase

A conventional brush border membrane preparation, obtained by divalent cation precipitation of homogenates of rabbit renal cortex, was analyzed by countercurrent distribution in an aqueous dextran:polyethylene glycol two-phase system. The resulting fractions were assayed for the presence of the Na+/H+ antiporter and for a variety of biochemical marker enzymes. This analysis revealed four physically distinct membrane populations (A-D). Population A consisted of two subpopulations, A' and A", which were enriched an average of 49-fold in maltase; they were also highly enriched in alkaline phosphatase, leucine aminopeptidase, and Na+/H+ antiporter. On the basis of their marker contents, populations A' and A" appear to represent highly purified, functional brush border membrane vesicles. Population B was enriched twofold in NADPH-cytochrome c reductase and population C was enriched 12-fold in galactosyltransferase. Populations B and C accounted for 25% of the protein in the starting material and appear to reflect contamination of the brush border membrane preparation by subpopulations of endoplasmic reticulum and Golgi fragments. Population D was enriched in Na+/H+ antiporter, alkaline phosphatase, leucine aminopeptidase, Na-K-ATPase, and acid phosphatase but not maltase, NADPH-cytochrome c reductase, galactosyltransferase, or succinate dehydrogenase. Its identity is unclear, and it might consist of a multiplicity of populations from different origins.

Isozyme characteristics of Caloscyphafulgens infested and pathogen-free spruce seed samples and use of alkaline phosphatase activity for qualitative and quantitative disease incidence assays

1981 ◽  
Vol 11 (2) ◽  
pp. 201-206
Author(s):  
Jack R. Sutherland ◽  
Ute Rink ◽  
E. E. McMullan ◽  
T. A. D. Woods
Keyword(s):  
Alkaline Phosphatase ◽  
Phosphatase Activity ◽  
Alkaline Phosphatase Activity ◽  
Gel Electrophoresis ◽  
Leucine Aminopeptidase ◽  
Disease Incidence ◽  
Prediction Equation ◽  
Qualitative And Quantitative ◽  
Phosphogluconate Dehydrogenase ◽  
Disease Free

Extracts of samples from Caloscyphafulgens infested and noninfested Sitka spruce (Piceasitchensis (Bong.) Carr.) seed lots and diseased and healthy seeds were separated by electrophoresis on polyacrylamide gels and stained for esterase (EC 3.1.1.1), leucine aminopeptidase (EC 3.4.1.1), acid phosphatase (EC 3.1.3.2), alkaline phosphatase (EC 3.1.3.1), glucose-6-phosphatase (EC 3.1.3.9), malate dehydrogenase (EC 1.1.1.37), isocitrate dehydrogenase (EC 1.1.1.42), 6-phosphogluconate dehydrogenase (EC 1.1.1.43) and alcohol dehydrogenase (EC 1.1.1.1). Several differences were detected between the isozyme patterns of disease-free and infested samples, but the main difference was the latter's high alkaline phosphatase activity. By using gel electrophoresis, (i) a qualitative analysis was developed, based on the presence or absence of alkaline phosphatase, to distinguish infested from disease-free seed lots, and (ii) the high alkaline phosphatase activity of infested samples was determined to be of pathogenic origin. By determining the alkaline phosphatase activity of samples with known numbers of diseased seeds, a prediction equation was derived relating enzyme activity and disease incidence. Correlation analyses showed significant (P = 0.01) correlations between disease incidence estimates obtained by this technique and plating of surface-sterilized seeds on water agar.

scholarly journals Enzymatic histochemistry of mouse kidney in plastic.

1987 ◽  
Vol 35 (4) ◽  
pp. 483-487 ◽  
Author(s):  
T P Pretlow ◽  
A S Lapinsky ◽  
L C Flowers ◽  
R W Grane ◽  
T G Pretlow
Keyword(s):  
Alkaline Phosphatase ◽  
Proximal Tubule ◽  
Leucine Aminopeptidase ◽  
Kidney Diseases ◽  
Mouse Kidney ◽  
Frozen Sections ◽  
Gamma Glutamyl Transpeptidase ◽  
Glutamyl Transpeptidase ◽  
Bowman's Capsule

Two-micrometer sections of methacrylate-embedded kidney were used to investigate the enzymatic activities of mouse kidney where the proximal tubule and Bowman's capsule from the same corpuscle were viewed in the same section. Alkaline phosphatase, acid phosphatase, 5'-nucleotidase, gamma-glutamyl transpeptidase, N-acetyl-beta-glucosaminidase, leucine aminopeptidase, alpha-naphthyl butyrate esterase, and adenosine triphosphatase activities were observed in the proximal tubule, but only 5'-nucleotidase, alpha-naphthyl butyrate esterase, and alkaline phosphatase were observed in the squamous portion of the parietal epithelium of Bowman's capsule. The use of methacrylate-embedded tissue allowed more precise localization of enzymatic activity than is possible with most frozen sections. This may provide interesting applications not only for characterization of kidney diseases but also for characterization of other normal and abnormal tissues.

scholarly journals The distribution of some hydrolases in glomeruli and tubular fragments prepared from rat kidney by zonal centrifugation

1971 ◽  
Vol 122 (5) ◽  
pp. 641-645 ◽  
Author(s):  
D. G. Taylor ◽  
R. G. Price ◽  
D. Robinson
Keyword(s):  
Alkaline Phosphatase ◽  
Acid Phosphatase ◽  
Gel Electrophoresis ◽  
Leucine Aminopeptidase ◽  
Rat Kidney ◽  
Kidney Cortex ◽  
Starch Gel Electrophoresis ◽  
Multiple Forms ◽  
Rat Kidney Cortex ◽  
Starch Gel

1. A collagenase digest of rat kidney cortex was separated into four bands by zonal centrifugation. 2. Two of these bands were shown by light-microscopy to contain glomeruli and tubular fragments, which were free from each other and well separated from other renal material. 3. Protein, N-acetyl-β-glucosaminidase, 5′-nucleotidase, l-leucine β-naphthylamidase, leucine aminopeptidase, acid phosphatase and alkaline phosphatase were assayed across the gradient. 4. The greater proportion of these enzyme activities was recovered in the tubular fragments and acid phosphatase was the only enzyme detected in significant amounts in the glomeruli. 5. Tubular fragments and glomeruli were sedimented and multiple forms of β-naphthylamidase, N-acetyl-β-glucosaminidase, acid phosphatase and alkaline phosphatase were investigated by starch-gel electrophoresis.

Anion-stimulated ATPase in locust rectal epithelium

1988 ◽  
Vol 66 (2) ◽  
pp. 431-438 ◽  
Author(s):  
R. A. Lechleitner ◽  
J. E. Phillips
Keyword(s):  
Alkaline Phosphatase ◽  
Plasma Membrane ◽  
Atpase Activity ◽  
Microsomal Fraction ◽  
Leucine Aminopeptidase ◽  
Mitochondrial Fraction ◽  
Mitochondrial Enzymes ◽  
Differential Centrifugation ◽  
Succinate Cytochrome C Reductase ◽  
Nacl Cotransport

The rectum, the main reabsorptive site in the locust excretory system, actively transports Cl−. This Cl− absorption is electrogenie, not dependent on Na+or [Formula: see text] and insensitive to inhibitors of NaCl cotransport or [Formula: see text] exchange. To determine if active Cl− transport across rectal epithelia might be due to an anion-stimulated ATPase, a microsomal fraction was obtained by differential centrifugation. Microsomal ATPase activity was stimulated in the following sequence: sulphite > bicarbonate > chloride. Maximal ATPase activity was obtained at 25 mM [Formula: see text] or 25 mM Cl−. Thiocyanate (10 mM) inhibited 90% of the anion-stimulated ATPase activity. The microsomal fraction was enriched in the plasma membrane markers, leucine aminopeptidase, alkaline phosphatase, 5′-nucleotidase, and γ-glutamyItranspeptidase, and had little contamination of the mitochondrial enzymes, succinate cytochrome c reductase and cytochrome oxidase. Na,K-ATPase was enriched in the mitochondrial fraction. Microscopic examination confirmed that basolateral membranes were associated with mitochondria following differential centrifugation, while the microsomal fraction contained little mitochondrial contamination. These results indicate the presence of an anion-stimulated ATPase activity that could be responsible for active Cl− transport across locust recta.

Morphological and histochemical observations onPolymorphus minutus(Goeze, 1782), with special reference to the body wall

Parasitology ◽  
1963 ◽  
Vol 53 (3-4) ◽  
pp. 663-685 ◽  
Author(s):  
D. W. T. Crompton
Keyword(s):  
Alkaline Phosphatase ◽  
Special Reference ◽  
Body Wall ◽  
Leucine Aminopeptidase ◽  
The Body ◽  
Structural Components ◽  
Histochemical Investigation ◽  
General Morphology ◽  
Additional Layer ◽  
University Of Edinburgh

1. Certain aspects of the general morphology ofPolymorphus minutusare described together with a detailed description of the body wall.2. An additional layer of the body wall, the epicuticle, has been demonstrated. It appears to consist of acid mucopolysaccharide and may have a function of protecting the parasite from the enzymes of its host.3. A histochemical investigation has been made of the layers of the body wall and it is concluded that lipoprotein is one of the main structural components.4. The distribution of the activity of the two enzymes, non-specific esterase and alkaline phosphatase, has been studied throughout the animal and the activity of a third enzyme, leucine aminopeptidase, has been detected in the body wall.5. It is suggested that all the layers of the body wall, with the exception of the cuticle and epicuticle, are of metabolic importance. The striped layer may be connected with absorption and the felt and radial layers may be involved in the further metabolism of absorbed compounds.6. The results obtained are used to formulate a possible structure of the surface of the parasite which would facilitate the absorption of nutrient substances through the body wall.I am grateful to Dr P. Tate for advice and encouragement during this work, Dr R. J. Tatchell for helpful discussions, and Dr D. L. Lee for criticising the manuscript and Mr T. M. Warwick, Department of Zoology, University of Edinburgh for providing material.

Effet de l'aflatoxine B1 sur les activités enzymatiques de Bacillus thuringiensis (Berliner)

1977 ◽  
Vol 23 (7) ◽  
pp. 931-932 ◽  
Author(s):  
P. Boutibonnes
Keyword(s):  
Alkaline Phosphatase ◽  
Bacillus Thuringiensis ◽  
Leucine Aminopeptidase ◽  
Sublethal Dose ◽  
Bacterial Cells ◽  
Aflatoxin B ◽  
Activités Enzymatiques

At 20 °C, aflatoxin B1, at a sublethal dose, decreases the activity of alkaline phosphatase (EC 3.1.3.1), α-glucosidase (EC 3.2.1.20), esterase (EC 3.1.1.1), chymotrypsin (EC 3.4.21.1), leucine aminopeptidase (EC 3.4.11.1), and phosphoamidase (EC 3.9.1.1) biosynthesis in Bacillus thuringiensis (Berliner).In contrast, at 41 °C no significant decrease was observed. At this temperature, the mycotoxin is not destroyed or metabolized and bacterial cells are resistant to the toxin.

High-molecular-mass alkaline phosphatase in serum and bile: nature and relationship with lipoprotein-X.

1981 ◽  
Vol 27 (6) ◽  
pp. 867-874 ◽  
Author(s):  
P M Crofton ◽  
A F Smith
Keyword(s):  
Alkaline Phosphatase ◽  
Enzyme Activity ◽  
Molecular Mass ◽  
Electrophoretic Mobility ◽  
Leucine Aminopeptidase ◽  
Current Knowledge ◽  
Normal Serum ◽  
High Molecular Mass ◽  
Variable Effect ◽  
Gamma Glutamyltransferase

Abstract Using immunoelectrophoresis and other techniques, we have demonstrated an association between lipoprotein-X and (a) alkaline phosphatase and (b) other enzymes originating from the hepatocyte membrane, namely gamma-glutamyltransferase and leucine aminopeptidase. The high-molecular-mass forms of these enzymes, in both serum and bile, were precipitated by lipoprotein-X antiserum but not by antisera to other plasma proteins. The activity of high-molecular-mass alkaline phosphatase in serum was positively correlated with lipoprotein-X and with lipoprotein-X-associated alkaline phosphatase, both assessed semi-quantitatively. On the other hand, many sera possessed high activities of high-molecular-mass alkaline phosphatase but no detectable lipoprotein-X. Incubation of serum with conjugated bile salts and with synthetic detergents, at concentrations which did not dissociate the high-molecular-mass enzymes, caused parallel alterations in the electrophoretic mobility of serum lipoprotein-X and its associated enzyme activity. Incubation of normal dialyzed hepatic bile with normal, lipoprotein-X-negative serum produced an alteration in electrophoretic mobility of biliary lipoprotein and its associated enzyme activity from anodal to cathodal in agar gel. Digestion with papain had a variable effect on the different enzymes in the complex, without affecting the lipoprotein moiety. Leucine aminopeptidase was removed most readily from the complex to give the low-molecular-mass form present in normal serum; gamma-glutamyltransferase dissociated somewhat less readily, and alkaline phosphatase was completely resistant to dissociation from the complex. These results are discussed in the light of current knowledge, and a hypothesis is proposed for the nature of the high-molecular-mass enzymes in serum and bile.

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