scholarly journals DISTRIBUTION OF ACID AND ALKALINE PHOSPHATASE ACTIVITY IN UNDEMINERALIZED SECTIONS OF THE RAT TIBIAL DIAPHYSIS

1969 ◽  
Vol 17 (12) ◽  
pp. 799-806 ◽  
Author(s):  
JON E. WERGEDAL ◽  
DAVID J. BAYLINK
Keyword(s):  
Alkaline Phosphatase ◽  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Alkaline Phosphatase Activity ◽  
Acid Phosphatase Activity ◽  
Strong Activity ◽  
Acid And Alkaline Phosphatase ◽  
Periosteal Cell ◽  
Rat Tibia ◽  
Tetracycline Labeling

The distribution of acid and alkaline phosphatase activity in the rat tibia has been studied in transverse sections sawed from fresh undemineralized diaphyses. The endosteal resorbing surfaces had the highest acid phosphatase activity as demonstrated with 50 mM α-naphthol phosphate as the substrate. Strong activity was present not only in osteoclasts and adjacent osteocytes but extracellularly lining Howship's lacunae. In areas of bone formation, moderate acid phosphatase activity was present in osteoblasts and young osteocytes. In addition, a zone of activity was found at the mineralizing front where mineralization is initiated. This active zone ( a) was separated from the active periosteal cell layer by a zone of inactive osteoid and ( b) in formol-calcium-fixed demineralized sections extended into young bone. The identity of the mineralizing front was confirmed by tetracycline labeling. The activity at the mineralizing front had the properties of an enzyme. Alkaline phosphatase activity demonstrated with naphthol ASTR phosphate was largely associated with the osteoblasts and other mesenchymal cells at forming surfaces.

scholarly journals HISTOCHEMICAL DEMONSTRATION OF ACID PHOSPHATASE ACTIVITY IN OSTEOCLASTS

1959 ◽  
Vol 7 (1) ◽  
pp. 39-41 ◽  
Author(s):  
M. S. BURSTONE
Keyword(s):  
Alkaline Phosphatase ◽  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Comparative Studies ◽  
Acid Phosphatase Activity ◽  
Azo Dye ◽  
Histochemical Demonstration ◽  
Accurate Localization ◽  
Acid And Alkaline Phosphatase ◽  
Cold Acetone

High acid phosphatase activity was observed in osteoclasts of several species using a reproducible azo-dye technique. High activity of two distinct enzymes, acid and alkaline phosphatase, are associated with osteoclasts and osteoblasts respectivey. Althouth frozen-dried tissues are recommended for definitive studies, the enzyme techniques used give satisfactory results with cold acetone-fixed tissues. The most accurate localization of acid phosphatase in osteoclasts in controlled comparative studies is obtained with double-embedded frozen-dried undecalcified tissues in conjunction with naphthol AS-phosphates.

scholarly journals ACID AND ALKALINE PHOSPHATASE IN WHITE CELLS DATA FOR THE LYMPHOCYTE AND THE POLYMORPHONUCLEAR LEUKOCYTE OF MAN AND THE RABBIT

Blood ◽  
1950 ◽  
Vol 5 (3) ◽  
pp. 267-277 ◽  
Author(s):  
W. F. HAIGHT ◽  
R. J. ROSSITER
Keyword(s):  
Alkaline Phosphatase ◽  
Acid Phosphatase ◽  
Statistical Analysis ◽  
Phosphatase Activity ◽  
Alkaline Phosphatase Activity ◽  
Human Cell ◽  
Human Lymphocyte ◽  
Polymorphonuclear Leukocyte ◽  
Cell Suspensions ◽  
Acid And Alkaline Phosphatase

Abstract 1. The acid and alkaline phosphatase activity has been determined on a series of suspensions of white cells obtained from both man and the rabbit by several different methods. 2. A statistical analysis of the results shows that for both species the alkaline phosphatase of white cell suspensions is confined chiefly to the polymorphonuclear leukocyte and the acid phosphatase is chiefly in the lymphocyte, although the polymonphonuclear leukocyte contains lesser concentrations of this enzyme also. 3. Although this qualitative distribution was the same for both species studied, quantitatively the rabbit differed from man. The activity of the alkaline phosphatase of the rabbit polymorphonuclear leukocyte was eight times that of the corresponding human cell, while the activity of the acid phosphatase of the human lymphocyte was more than twice that of rabbit lymphocyte.

PHOSPHOMONOESTERASE ACTIVITY IN THE LIFE-CYCLE STAGES OF SCHISTOCERCA GREGARIA

1968 ◽  
Vol 100 (6) ◽  
pp. 649-655 ◽  
Author(s):  
S. N. H. Naqvi ◽  
Shahid H. Ashrafi ◽  
M. A. H. Qadri
Keyword(s):  
Alkaline Phosphatase ◽  
Acid Phosphatase ◽  
Embryonic Development ◽  
Phosphatase Activity ◽  
Alkaline Phosphatase Activity ◽  
Acid Phosphatase Activity ◽  
Schistocerca Gregaria ◽  
Adult Males ◽  
First Instar ◽  
Almost All

AbstractThe acid and alkaline phosphatase activity was measured in the developing egg and in the alimentary canal of aging nymphs as well as adult males and females of different ages. Para-nitrophenol was used as colorimetric standard and disodium p-nitrophenyl phosphate as substrate. Activity was measured in terms of micromoles of p-nitrophenol liberated from the substrate as a result of enzyme action.Acid phosphatase activity was noticed to increase with the embryonic development and was higher than in the case of alkaline phosphatase. The alkaline phosphatase activity was lowest in the freshly laid egg, but increased more sharply than acid phosphatase during embryonic development.The activity of both the acid and alkaline phosphatases was highest in the first instar and declined gradually to the fifth instar. The activity of acid phosphatase was higher than alkaline phosphatase in all stages except the first instar where it was almost equal. The activity of both the enzymes was higher during the intermoulting period and declined at each moult indicating a hormone–enzyme relationship.In adults, activity of both the enzymes increased up to the maturation period after which the activity gradually decreased. Acid phosphatase activity was generally higher in males whereas alkaline phosphatase activity was generally higher in females. In almost all cases, the acid phosphatase activity was found to be higher than the alkaline phosphatase.

Phosphatase Activity in Some Species of Marine Phytoplankters

1965 ◽  
Vol 22 (3) ◽  
pp. 793-799 ◽  
Author(s):  
N. J. Antia ◽  
A. Watt
Keyword(s):  
Alkaline Phosphatase ◽  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Alkaline Phosphatase Activity ◽  
Pure Culture ◽  
Acid Phosphatase Activity ◽  
Phaeodactylum Tricornutum ◽  
Skeletonema Costatum ◽  
Isochrysis Galbana ◽  
Nitrophenyl Phosphate

Evidence has been obtained for acid phosphatase activity (on p-nitrophenyl phosphate as substrate) at pH 4.8 in cell-free extracts of Phaeodactylum tricornutum, Skeletonema costatum, Cyclotella nana, Monochrysis lutheri, Isochrysis galbana, and Dunaliella tertiolecta grown photo-autotrophically in pure culture. No alkaline phosphatase activity at pH 10.5 was observed.

Scanning electron microscopy, whole-mount histology, and histochemistry of two anodontine glochidia (Bivalvia: Unionidae)

1996 ◽  
Vol 74 (11) ◽  
pp. 1964-1973 ◽  
Author(s):  
M. Pekkarinen
Keyword(s):  
Methylene Blue ◽  
Alkaline Phosphatase ◽  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Alkaline Phosphatase Activity ◽  
Acid Phosphatase Activity ◽  
Neutral Lipids ◽  
Periodic Acid ◽  
Critical Point Drying ◽  
Electrolyte Uptake

Intramarsupial glochidia of Anodonta anatina (L.) and Pseudanodonta complanata (Rossmässler) were studied in southern Finland. Material staining positively with periodic acid – Schiff's reagent (PAS), neutral lipid reserves, and acid phosphatase activity have different distributions in the mantle of the two species. Moreover, the mucous covering of the mantle of the two glochidia behaves differently on critical-point drying. The presence of microvilli with alkaline phosphatase activity on the mantle surface and acid phosphatase activity in the mantle cells in both glochidia suggest that the mantle plays a role in nutrient uptake and digestion and possibly also in electrolyte uptake. The primordia of the stomach, digestive diverticula, and intestine, at least in A. anatina glochidia, contain neutral lipids and exhibit acid phosphatase activity: In A. anatina glochidia, a microvillous layer with alkaline phosphatase activity continues from the ventral walls of the lateral pits to the suspected kidney diverticula. In both glochidia, there may be three pairs of rudimentary ganglia, which do not stain with methylene blue. The eight ciliated sense organs of the glochidia are methylene blue- and PAS-positive and they exhibit succinate dehydrogenase and acid phosphatase activity. In each mantle lobe, the enveloping cell of the dorsal ciliary organ is interconnected with those of the ventral triad via a cellular fold or "tract," and the ciliated central cells of the organs send axons towards each other.

Absence of Measurable Leukocyte Alkaline Phosphatase Activity from Leukocytes of Patients with Chronic Granulocytic Leukemia

1970 ◽  
Vol 16 (9) ◽  
pp. 798-799 ◽  
Author(s):  
Lawrence R DeChatelet ◽  
M Robert Cooper ◽  
Charles E McCall
Keyword(s):  
Alkaline Phosphatase ◽  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Alkaline Phosphatase Activity ◽  
Acid Phosphatase Activity ◽  
Alkaline Ph ◽  
Chronic Granulocytic Leukemia ◽  
Leukocyte Alkaline Phosphatase ◽  
Ph Range ◽  
Granulocytic Leukemia

Abstract Leukocyte phosphatase activity was determined over a broad pH range. Using this procedure, we found no alkaline phosphatase activity in leukocytes from three patients with chronic granulocytic leukemia. The low values usually reported for this disease are actually attributable to acid phosphatase activity, which is slight but measurable at alkaline pH.

Effect of Alkaline and Acid Phosphatases on Clotting:

1966 ◽  
Vol 15 (03/04) ◽  
pp. 365-380 ◽  
Author(s):  
P. G Iatridis ◽  
J. H Ferguson
Keyword(s):  
Alkaline Phosphatase ◽  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Alkaline Phosphatase Activity ◽  
Inhibitory Effect ◽  
Factor Ix ◽  
Acid Phosphatases ◽  
Acid And Alkaline Phosphatase ◽  
Direct Inhibitory Effect ◽  
Alkaline And Acid Phosphatases

SummaryAlkaline phosphatase is found to enhance the activation of factor IX by SF. The correlation of the distribution of alkaline phosphatase in electrophoretic fractions with the clotting tests suggest that the “beta” fraction contains the responsible factor for the acceleratory effect of alkaline phosphatase on clotting.Acid phosphatase, while not exerting a direct inhibitory effect on SF, does enhance the plasmatic anti-SF activity. The “beta” and “F-gamma” fractions seem to contain the responsible factor of acid phosphatase for the plasmatic anti-SF enhancement.SF preparation has no acid or alkaline phosphatase activity.A tentative schema is proposed to explain the effects of acid and alkaline phosphatase on clotting.

scholarly journals THE FINE STRUCTURAL LOCALIZATION OF ALKALINE AND ACID PHOSPHATASE ACTIVITY IN THE RAT SUBMANDIBULAR GLAND

1968 ◽  
Vol 16 (9) ◽  
pp. 572-581 ◽  
Author(s):  
BRUCE I. BOGART
Keyword(s):  
Alkaline Phosphatase ◽  
Plasma Membrane ◽  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Alkaline Phosphatase Activity ◽  
Acid Phosphatase Activity ◽  
Myoepithelial Cell ◽  
Structural Localization ◽  
Pinocytotic Vesicles ◽  
Rat Submandibular Gland

The lead capture method was employed to study the fine structural localization of nonspecific phosphatase activity in the rat submandibular gland. Alkaline phosphatase activity was observed in association with the plasma membrane and pinocytotic vesicles of the myoepithelial cell. A polarity in the distribution of alkaline phosphatase activity was described along the myoepithelial cell process. More reaction product was observed in association with the plasma membrane on the parenchymal surface than on the plamsa membrane on the stromal surface, where reaction product was confined mostly to the pinocytotic vesicles. Activity was evenly distributed over both surfaces of the portion of the myoepithelial cell characterized by the nucleus. Activity was also observed to be associated with pinocytotic vesicles of the endothelial cells and the plasma membrane of erythrocytes. No activity was observed in association with the ductal elements. Acid phosphatase activity was associated with membrane-bound structures in the acini and ducts. These structures took the form of lipofuscin granules in the acini and either multivesicular or dense bodies in the ducts.

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