scholarly journals INHIBITION OF RENAL ACID PHOSPHATASE AND ARYL SULFATASE ACTIVITY BY GLUTARALDEHYDE FIXATION

1971 ◽  
Vol 19 (7) ◽  
pp. 449-451 ◽  
Author(s):  
BENGT ARBORGH ◽  
JAN L. E. ERICSSON ◽  
HEIKKI HELMINEN
Keyword(s):  
Acid Phosphatase ◽  
Glutaraldehyde Fixation ◽  
Aryl Sulfatase ◽  
Sulfatase Activity

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.

Cytochemical study of lysosomal aryl sulfatase and acid phosphatase activities in rat retina

Micron (1969) ◽  
1979 ◽  
Vol 10 (3) ◽  
pp. 187-188
Author(s):  
Edward Essner ◽  
Gregg M. Gorrin ◽  
Richard A. Griewski
Keyword(s):  
Acid Phosphatase ◽  
Cytochemical Study ◽  
Aryl Sulfatase ◽  
Rat Retina ◽  
Phosphatase Activities

scholarly journals THE DEMONSTRATION OF ACID HYDROLASE ACTIVITIES IN THE INCLUSION BODIES OF TYPE II ALVEOLAR CELLS AND OTHER LYSOSOMES IN THE RABBIT LUNG

1968 ◽  
Vol 16 (2) ◽  
pp. 102-109 ◽  
Author(s):  
SIDNEY GOLDFISCHER ◽  
YUTAKA KIKKAWA ◽  
LEE HOFFMAN
Keyword(s):  
Acid Phosphatase ◽  
Inclusion Bodies ◽  
Active Sites ◽  
Cytoplasmic Inclusion ◽  
Alveolar Epithelial Cells ◽  
Type Ii ◽  
Alveolar Cells ◽  
Rabbit Lung ◽  
Aryl Sulfatase ◽  
Alveolar Epithelial

Type II alveolar epithelial cells show high levels of acid phosphatase, aryl sulfatase B and β-glucuronidase activities. In formalin- and glutaraldehyde-fixed rabbit lung acid phosphatase and aryl sulfatase B activities were demonstrated in the cytoplasmic inclusion bodies, supporting their identification as lysosomes. Type II cells differ from alveolar macrophages in their levels of hydrolase activity and the fine structure of their active sites.

A particulate fraction from Neurospora crassa exhibiting aryl sulfatase activity

1971 ◽  
Vol 142 (2) ◽  
pp. 623-632 ◽  
Author(s):  
Walter A. Scott ◽  
Kenneth D. Munkres ◽  
Robert L. Metzenberg
Keyword(s):  
Neurospora Crassa ◽  
Particulate Fraction ◽  
Aryl Sulfatase ◽  
Sulfatase Activity

Preliminary Studies on Heterotopic Calcinosis

1970 ◽  
Vol 28 ◽  
pp. 242-243
Author(s):  
J.R. Scott ◽  
R.B. Marshall ◽  
D.K. Roberts
Keyword(s):  
Alkaline Phosphatase ◽  
Acid Phosphatase ◽  
Connective Tissue ◽  
Cell Population ◽  
Giant Cells ◽  
Tumoral Calcinosis ◽  
Fibrous Connective Tissue ◽  
Enzyme Cytochemistry ◽  
Calcium Salts ◽  
Aryl Sulfatase

Interstitial calcinosis and tumoral calcinosis lesions were studied ultrastructurally and with the use of enzyme cytochemistry. Technics for alkaline phosphatase, acid phosphatase, atpase and aryl sulfatase were utilized after removal of calcium salts with EDTA.Granular elements were seen in both lesions. These granules were seen to lie in cystic spaces of the lesions (Figure 1). Also seen were aggregates of these granules which had apparently calcified (Figure 2). The lesion of tumoral calcinosis had many multinuclear giant cells present peripheral to the cystic spaces with macrophages contributing to the cell population. The lesions all had a pseudocapsule of fibrous connective tissue and “active” connective tissue cells were seen near the cystic space.

The blood leukocytes of Bufo alvarius: a light, phase-contrast, and histochemical study

1979 ◽  
Vol 57 (2) ◽  
pp. 314-322 ◽  
Author(s):  
M. Samuel Cannon ◽  
A. M. Cannon
Keyword(s):  
Acid Phosphatase ◽  
Phase Contrast ◽  
Periodic Acid ◽  
Hydrolytic Enzymes ◽  
Neutral Red ◽  
Nonspecific Esterase ◽  
Alkaline Phosphatases ◽  
Blood Leukocytes ◽  
Periodic Acid Schiff ◽  
Aryl Sulfatase

Blood leukocytes of Bufo alvarius were studied by light and phase-contrast microscopy and histochemical techniques for the localization of glycogen and several hydrolytic enzymes, i.e., acid and alkaline phosphatases, nonspecific esterase, beta-glucuronidase, aryl-sulfatase, and myeloperoxidase (peroxidase). Neutrophils were the only leukocytes to demonstrate alkaline phosphatase activity, while beta-glucuronidase and aryl-sulfatase were not observed in any leukocytes. Periodic acid – Schiff (PAS) positive granules and granules containing hydrolytic enzymes occurred in varying amounts in leukocytes. In eosinophils, most glycogen was associated with smaller granules, while the larger refractile granules were PAS negative. Small lymphocytes were myeloperoxidase (peroxidase) negative. The present study agrees with previous investigations in mammals which indicate that specific granules in granulocytes may be PAS positive as well as contain one or more hydrolytic enzymes. In small lymphocytes of B. alvarius, PAS positive and acid phosphatase positive granules correspond to neutral red granules seen in supravital films. Furthermore, the appearance and histochemical reactivity of acid phosphatase granules in mature neutrophils, metamyelocytes, and late myelocytes correspond closely with the appearance and number of specific neutrophilic granules seen in Wright–Giemsa preparations and with PAS positive granules.

Sign in / Sign up

Export Citation Format

Share Document