scholarly journals HISTOCHEMISTRY OF LYSOSOMES IN RAT HEART MUSCLE

1967 ◽  
Vol 15 (10) ◽  
pp. 596-599 ◽  
Author(s):  
R. ABRAHAM ◽  
MARGARET MORRIS ◽  
JENNIFER SMITH
Keyword(s):  
Enzyme Activity ◽  
Acid Phosphatase ◽  
Heart Muscle ◽  
Rat Heart ◽  
Lysosomal Hydrolases ◽  
Aryl Sulfatase ◽  
Sulfatase Activity ◽  
Triton X

Rat heart muscle was studied histochemically by the naphthol and lead methods for hydrolases (acid phosphatase, esterase, β-glucuronidase and aryl sulfatase). Activity of the enzymes studied is demonstrable in granules which by their staining properties are identified as lysosomes. These organelles are usually perinuclear in location and display variable amounts of enzyme activity. The heart lysosomes in chloroquine-treated rats are enlarged and aggregated together. The effects of the detergent Triton X-100 on the lysosomal hydrolases are discussed.

scholarly journals Lysosomal enzymes and vitamin E deficiency

1967 ◽  
Vol 21 (1) ◽  
pp. 147-154 ◽  
Author(s):  
J. Bunyan ◽  
J. Green ◽  
A. T. Diplock ◽  
D. Robinson
Keyword(s):  
Enzyme Activity ◽  
Acid Phosphatase ◽  
Lysosomal Enzymes ◽  
Hydrolytic Activity ◽  
Liver Necrosis ◽  
Lysosomal Hydrolases ◽  
Vitamin E Deficiency ◽  
Nitrophenyl Phosphate ◽  
Liver And Kidney ◽  
Testicular Degeneration

1. The activities of several lysosomal hydrolases have been measured in tissues of rats with nutritional liver necrosis. Incipient or actual liver necrosis did not alter total, free or unsedimentable activities of cathepsin, β-glucuronidase, β-galactosidase or acid phosphatase of liver and kidney. Free hydrolytic activity towards p-nitrophenyl phosphate was slightly raised in liver, and serum β-galactosidase and β-glucuronidase were moderately elevated. These results suggest that lysosomal hydrolases are not directly implicated in the causation of liver necrosis.2. Testicular degeneration was studied with reference to changes in β-giucuronidase activity. This enzyme activity, total, free and unsedimentable, was raised in deficient rat testis at 6 months old and did not decline even after a year. Raised values were also found in serum.

scholarly journals DEMONSTRATION OF ACID PHOSPHATASE ACTIVITY USING 1-ACETYL-3-INDOLYL PHOSPHATE AS SUBSTRATE

1971 ◽  
Vol 19 (3) ◽  
pp. 175-181 ◽  
Author(s):  
MASANDO HAYASHI
Keyword(s):  
Enzyme Activity ◽  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Acid Phosphatase Activity ◽  
Lead Ions ◽  
Lead Salt ◽  
Male Rats ◽  
Cytochemical Demonstration ◽  
Liver And Kidney ◽  
Triton X

A simultaneous coupling azo-indoxyl method for the cytochemical demonstration of acid phosphatase activity using p-toluidine salt of 1-acetyl-3-indolyl phosphate is described. A satisfactory staining for the enzyme activity was obtained following incubation of formol-calcium-fixed frozen sections for 30 min at 25°C in a medium containing 1 mM each of the substrate and hexazonium pararosanilin and adjusted to pH 4.5-5.0 with acetate buffer. The distribution of acid phosphatase activity demonstrated by this method was identical with that obtained either by Gomori's technique using β-glycerophosphate as substrate or by the Barka and Anderson's naphthol AS-BI phosphate-hexazonium pararosanilin method in several tissues of male rats so far examined. However, the adrenal enzyme activity was most prominent in the medulla with 1-acetyl-3-indolyl phosphate and β-glycerophosphate but it was more marked in the cortex with naphthol AS-BI phosphate. An advantage of using 1-acetyl-3-indolyl phosphate as substrate is that the same compound can be used for comparing azo-indoxyl and lead-salt methods. Effects of phospholipase C and Triton X-100 on staining for acid phosphatase were tested by pretreating fixed rat liver and kidney sections with these agents and incubating them in the medium containing 1-acetyl-3-indolyl phosphate and either hexazonium pararosanilin or lead ions as a coupler. The pretreatment did not change discrete lysosomal staining, as seen in untreated controls, using pararosanilin as a coupler, but greatly modified the staining using lead ions. The results indicate that the preciseness of staining for acid phosphatase with lead-salt method is highly dependent on some lipid material which attracts lead in tissues and that appropriately devised azo dye or azo-indoxyl methods demonstrate enzyme sites more accurately than lead-salt method.

scholarly journals ULTRASTRUCTURAL AND CYTOCHEMICAL OBSERVATIONS ON B-16 AND HARDING-PASSEY MOUSE MELANOMAS THE ORIGIN OF PREMELANOSOMES AND COMPOUND MELANOSOMES

1968 ◽  
Vol 16 (5) ◽  
pp. 299-319 ◽  
Author(s):  
ALEX B. NOVIKOFF ◽  
ARLINE ALBALA ◽  
LUIS BIEMPICA
Keyword(s):  
Electron Microscopy ◽  
Endoplasmic Reticulum ◽  
Enzyme Activity ◽  
Acid Phosphatase ◽  
Light Microscopy ◽  
Lysosomal Enzyme ◽  
Smooth Endoplasmic Reticulum ◽  
Aryl Sulfatase ◽  
Thiamine Pyrophosphatase ◽  
Inosine Diphosphatase

The B-16 and Harding-Passey mouse melanomas were studied by light microscopy (tyrosinase, acid phosphatase, aryl sulfatase, thiamine pyrophosphatase and inosine diphosphatase activities) and electron microscopy (morphology and tyrosinase and acid phosphatase activities). Lysosomal enzyme activity is present in individual premelanosomes and melanosomes as well as in compound melanosomes. Acid phosphatase and tyrosinase activities are present in a Golgi-associated system of smooth endoplasmic reticulum (GERL) and small vesicles related to it. The acid phosphatase and tyrosinase activities of premelanosomes, and morphologic appearances, support the hypothesis that the granules arise from GERL. On the basis of the evidence presented, it is suggested that compound melanosomes arise within melanoma cells by autophagy.

Smartphone Based Highly Sensitive Visualized Detection of Acid Phosphatase Enzyme Activity

2021 ◽  
Author(s):  
Rui Li ◽  
Yanan Sun ◽  
Lihua Jin ◽  
Xiaohong Qiao ◽  
Cong Li ◽  
...  
Keyword(s):  
Enzyme Activity ◽  
Acid Phosphatase ◽  
Point Of Care ◽  
Rapid Development ◽  
Practical Application ◽  
Fast Analysis ◽  
Highly Sensitive ◽  
Visualized Detection ◽  
Sensitive Method ◽  
Phosphatase Enzyme

With the rapid development of point-of-care (POC) technologies, the improvement of sensitive method featured with fast analysis and affordable devices has become an emerging requirement for the practical application. In...

Changes in ECG and enzyme activity in rat heart after myocardial infarction: effect of TPP and MnCl2

2008 ◽  
Vol 64 (2) ◽  
pp. 93-101 ◽  
Author(s):  
A. Tylicki ◽  
J. Czerniecki ◽  
A. Godlewska ◽  
M. Kieliszek ◽  
T. Zebrowski ◽  
...  
Keyword(s):  
Myocardial Infarction ◽  
Enzyme Activity ◽  
Rat Heart

scholarly journals Enzyme Histochemical Studies of Adipose Tissue in Porcine Yellow Fat Disease

1974 ◽  
Vol 11 (6) ◽  
pp. 465-476 ◽  
Author(s):  
L. H. J. C. Danse ◽  
W. A. Steenbergen-Botterweg
Keyword(s):  
Enzyme Activity ◽  
Adipose Tissue ◽  
Acid Phosphatase ◽  
Nonspecific Esterase ◽  
Cell Structures ◽  
Increased Activity

Adipose tissue of piglets with yellow fat disease had increased activity of nonspecific esterase, 5-nucleotidase, and acid phosphatase. Since these enzymes are associated with different cell structures and damage to these structures can result in increased enzyme activity, they are criteria for pathogenetic study of yellow fat disease.

scholarly journals Lysosomal enzymes and vitamin E deficiency

1967 ◽  
Vol 21 (1) ◽  
pp. 127-136 ◽  
Author(s):  
J. Bunyan ◽  
J. Green ◽  
A. T. Diplock ◽  
D. Robinson
Keyword(s):  
Acid Phosphatase ◽  
Subcellular Distribution ◽  
Subcutaneous Tissue ◽  
Hydrolytic Activity ◽  
Breast Muscle ◽  
Lysosomal Hydrolases ◽  
Exudative Diathesis ◽  
Glucuronidase Activity ◽  
Deficiency Diseases ◽  
Increased Activity

1. The activities of several lysosomal hydrolases were measured in the tissues of chicks suffering from nutritional muscular dystrophy, encephalomalacia or exudative diathesis.2. In dystrophic breast muscle, β-glucuronidase was raised five- to six-fold, cathepsin fourfold and acid phosphatase 1.5-fold. No change was found in the subcellular distribution of β-glucuronidase.3. Chicks with encephalomalacia showed no changes in the β-glucuronidase, β-galactosidase, acid phosphatase or β-acetylglucosaminase activities of cerebellum or brain. Subcellular distribution of β-glucuronidase and β-galactosidase in these tissues was also unchanged.4. In exudative diathesis, hydrolases were found in the exudate, and there was increased activity in the subcutaneous tissue first showing haemorrhages. Increased hydrolytic activity was found in liver, spleen and kidney. Breast muscle was not always affected by the exudative condition, but, when it too degenerated, its hydrolase activity increased.5. β-Glucuronidase activity was measured in the serums of chicks suffering from each of the three deficiency diseases. None of the diseases caused a rise in activity.

scholarly journals Mucin biosynthesis. Properties of a bovine tracheal mucin β-6-N-acetylglucosaminyltransferase

1985 ◽  
Vol 227 (2) ◽  
pp. 405-412 ◽  
Author(s):  
P W Cheng ◽  
W E Wingert ◽  
M R Little ◽  
R Wei
Keyword(s):  
Enzyme Activity ◽  
Freezing Point ◽  
Cetylpyridinium Chloride ◽  
Sodium Dodecyl ◽  
Sodium Deoxycholate ◽  
Gas Chromatography Mass Spectrometry ◽  
Tween 20 ◽  
Group A ◽  
Michaelis Constants ◽  
Triton X

We have characterized a bovine tracheal mucin beta-6-N-acetylglucosaminyltransferase that catalyses the transfer of N-acetylglucosamine from UDP-N-acetylglucosamine to the C-6 of the N-acetylgalactosamine residue of galactosyl-β 1→3-N-acetylgalactosamine. Optimal enzyme activity was obtained between pH 7.5-8.5, at 5mM-MnCl2, and at 0.06-0.08% (v/v) Triton X-100 (or Nonidet P-40), or 0.5-5.0% (v/v) Tween 20. Ba2+, Mg2+ and Ca2+ could partially replace Mn2+, but Co2+, Fe2+, Cd2+ and Zn2+ could not. Sodium dodecyl sulphate, cetylpyridinium chloride, sodium deoxycholate, octyl beta-D-glucoside, digitonin and alkyl alcohols were less effective in enhancing enzyme activity, and dimethyl sulphoxide was ineffective. The apparent Michaelis constants were 1.25 mM for UDP-N-acetylglucosamine, 0.94-3.34 mM for freezing-point-depressing glycoprotein and 0.19 mM for periodate-treated blood-group-A porcine submaxillary mucin. Asialo ovine submaxillary mucin could not serve as the glycosyl acceptor. The structure of the 14C-labelled oligosaccharide obtained by alkaline-borohydride treatment of the product was identified as Gal beta 1→3(Glc-NAc beta 1→6)N-acetylgalactosaminitol by beta-hexosaminidase treatment, gas chromatography-mass spectrometry and 1H-n.m.r. (270 MHz) analysis. The enzyme is important in the regulation of mucin oligosaccharide biosynthesis.

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