Journal of Histochemistry & Cytochemistry

MORETTI, GIUSEPPI; ADACHI, KENJI; ELLIS, RICHARD A.

doi: 10.1177/8.4.237pmid: 14424075

Using Semi-quantitative and photometric techniques, regional variations in the activity of acid phosphatase and Tween esterase have been demonstrated in the epidermis of the chimpanzee and macaque. The observed differences cannot be directly correlated with regional changes in the morphology of the epidermis. It is suggested that similar variability in a multiplicity of enzymes may account for the structural differences, and obscure specific correlations with the two enzymes we have studied.

MUKHERJI, MRITYUNJOY; DEB, CHANDICHARAN

doi: 10.1177/8.4.242pmid: 14425084

Neutral lipids (Sudan positive substances), unsaturated lipids and plasmalogen were demonstrated in liver, fat body, kidney, adrenals, testis, intestine and cardiac muscle of toad (Bufo melanostictus) during hibernation (February), post-hibernation (April), breeding season (August) and prehibernation (November).In liver and fat body maximum sudanophilia has been observed during November, with decrease during February and complete disappearance during April. In August it began to accumulate again. Unsaturated lipid and plasmalogen were absent in February and rose to a maximum during August. These changes indicate that fat is being utilized during hibernation. In testis a maximum of unsaturated lipid and plasmalogen have been observed during August and a minimum during February. In February accumulation of neutral fat has been observed in the intertubular and intratubular space of this organ. In adrenals maximum sudanophilia, unsaturated lipid and plasmalogen have been observed during February, with minimums during August. These changes in testes and adrenals indicate hypofunction of the glands during hibernation. In kidney and intestine a maximum of unsaturated lipid and plasmalogen has been seen during August, with a minimum during February; cardiac muscle showed very little alteration in the lipid fractions. These changes have been ascribed to seasonal alteration in the activity of the organs; the heart, being a vital one, showed minimum alteration.

TAYLOR, KENNETH B.

doi: 10.1177/8.4.248pmid: 13837171

1. The chromatographic behaviour of 22 closely related N-alkyl thionins in a number of solvent systems is described.2. Details are given of the separation of commercial mixtures of the azures into their components and the application of this to the analysis of Romanowsky stains.3. A table giving the Rf equivalents and absorption maxima of the dyes is appended and the additive effect of alkyl substitution is discussed.

GLENNER, GEORGE G.; WEISSBACH, HERBERT; REDFIELD, BETTY G.

doi: 10.1177/8.4.258pmid: 13706042

The availability of synthetic indolyl-3-acetaldehyde has made possible the determination of the mechanism of reduction of tetrazolium salts in the tryptamine-tetrazolium technique for the demonstration of monoamine oxidase activity. This aldehyde, formed as the result of the enzymatically catalyzed oxidative deamination of tryptamine, directly reduces sensitive tetrazolium salts to localize monoamine oxidase activity in tissue sections. No implication of a diaphorase-like system in the reduction of the tetrazoles was found.The possibility of a pigment precursor being formed as the result of the oxidation of the indolyl aldehyde during tetrazole reduction is discussed and the utilization of a similar scheme of nonenzymatic reduction of an indicator dye for demonstrating both oxidative and hydroytic enzyme systems is presented.

ADAMS, C. W. M.

doi: 10.1177/8.4.262pmid: 13791775

1. The reactions of tissues with OsO4 and the Swank-Davenport KClO3-OsO4 (Marchi) reagent have been studied by blockade of the reducing groups of unsaturated lipid, protein and polysaccharide. Only blockade of the —CH=CH— bond prevented osmiophilia after brief staining (18 hr.).2. Tissue-protein is neither stained nor demonstrably impregnated after brief treatment with OsO4.3. Chromatographic separation of degenerating myelin revealed that the Marchi-substance is eluted in the esterified cholesterol fraction.4. Unsaturated lipid but not protein or polysaccharide are stained by brief treatment with OsO4. The Marchi reaction distinguishes hydrophilic from hydrophobic unsaturated lipid.

RUTENBURG, ALEXANDER M.; GOLDBARG, JULIUS A.; RUTENBURG, SELMA H.; LANG, RUTH T.

doi: 10.1177/8.4.268pmid: 14440354

A histochemical method for the demonstration of α-d-glucosidase is presented. The procedure and the problems encountered in its development are discussed. Surveys of mammalian tissues showed that this enzyme is generally demonstrable by this method only in the mucosa of the duodenum and upper jejunum and in the kidney cortex. Starvation resulted in decreased enzymatic activity in the intestinal mucosa, whereas increased activity was observed after the ingestion of food.

EMMART, E. W.; TURNER, W. A.

doi: 10.1177/8.4.273pmid: 13820186

I. Streptococcal hyaluronidase and the bacterium Streptococcus hemolyticus, Group C, strain 7, have been identified within the same tissue section by tagging the former with its specific antibody coupled to yellow-green fluorescein and the latter with Group C antisera coupled to acid rhodamine B (C.I. No. 45100).2. The methods used above suggest a means of studying the absorption and activity of other antigenic enzymes and toxins elaborated during the course of infection.

FORAKER, ALVAN G.

doi: 10.1177/8.4.284pmid: 13823859

Sections from ten cases of adenocarcinoma of the human colon were stained with methylene blue and with light green SF in a range of pH. Staining intensity of various cellular structures in normal and neoplastic mucosa was recorded on an arbitrary scale. This procedure is said to assist in characterization of proteins. Nuclear structures stained more intensely with methylene blue in alkaline ranges. Mitotic figures in carcinoma retained affinity for methylene blue in relatively acid ranges when other nuclear structures stained weakly. Cytoplasmic staining with light green increased in acid ranges. Only mucin showed some metachromasia. None of the findings sharply differentiated between normal and carcinoma cells.

FULLMER, HAROLD M.

doi: 10.1177/8.4.290pmid: 13825625

WATTENBERG, LEE W.; LEONG, J. LIONEL

doi: 10.1177/8.4.296pmid: 13843158

Coenzyme Q10 and menadione have been shown to enhance the succinic dehydrogenase activity of rat liver homogenates and frozen sections as measured quantitatively by the reduction of INT. Increased formazan deposition as estimated by visual examination was also found in sections of liver and other tissues in comparable experiments with the two quinones in which the tetrazolium salt Nitro-BT was employed.Extraction of sections with acetone decreased the succinic dehydrogenase activity of liver sections by approximately two-thirds of that present in nonextracted sections as measured by INT reduction. The addition of coenzyme Q10 or menadione restored the activity to essentially that present in nonextracted sections incubated in the presence of the same constituents. These data suggest that a quinone, presumably coenzyme Q10, acts as an intermediate electron transport agent between succinic dehydrogenase and INT or Nitro-BT.The effects of coenzyme Q10 and menadione on the activities of diphosphopyridine nucleotide (DPNH) diaphorase, triphosphopyridine nucleotide (TPNH) diaphorase, α-glycerophosphate dehydrogenase and monoamine oxidase, all of which are demonstrable by tetrazolium salt reduction procedures, have been studied. Two of these enzymes, TPNH diaphorase and monoamine oxidase, show no significant enhancement of activity in the presence of coenzyme Q10, and a relatively slight enhancement in the presence of menadione. α-Glycerophosphate dehydrogenase shows a pattern of enhancement comparable to that of succinic dehydrogenase. DPNH diaphorase activity, while enhanced by both of the quinones, shows a lesser degree than is found with the succinic dehydrogenase and α-glycerophosphate dehydrogenase systems.The diverse effects of coenzyme Q10 and menadione on the five enzyme systems investigated in the present work indicate that the two quinones do not simply act as nonspecific intermediate electron carriers between dehydrogenase system and tetrazolium salt, but that they enhance enzyme activity by a more specific interaction with some component of the enzyme system.