The role of acid phosphatase activity during enzymic dephosphorylation of phytates byAspergillus niger phytase

1993 ◽  
Vol 9 (1) ◽  
pp. 117-119 ◽  
Author(s):  
K. Żyta
Keyword(s):  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Acid Phosphatase Activity

Role of enzymes in the mechanism of shell penetration by the muricid gastropod, Thais lapillus (L.)

1977 ◽  
Vol 55 (11) ◽  
pp. 1846-1857 ◽  
Author(s):  
Roy S. Webb ◽  
A. S. M. Saleuddin
Keyword(s):  
Acid Phosphatase ◽  
Carbonic Anhydrase ◽  
Phosphatase Activity ◽  
Acid Phosphatase Activity ◽  
Carbonic Anhydrase Activity ◽  
Marker Enzyme ◽  
Biochemical Activity ◽  
Significant Difference ◽  
Muricid Gastropods

The role of the boring organ in the mechanism of shell penetration by Thais lapillus (L.), a muricid gastropod, has been investigated by cytochemistry and biochemistry. Sites of acid phosphatase and carbonic anhydrase activity were localized and the biochemical activities of these enzymes were measured in the boring organ of both nonboring and actively boring animals. The lysosomal marker enzyme, acid phosphatase, was investigated to assess the role of lysosomes in the boring mechanism. Acid phosphatase activity was localized on the microvillar membranes of the epithelial cells of the boring organ. There was no significant difference in the biochemical activity of acid phosphatase between actively boring and nonboring specimens. Carbonic anhydrase was localized prominently in the epithelium of the boring organ. The microvilli showed no localization but all other regions of the epithelium were dominated by reaction product. The boring organ demonstrated high levels of carbonic anhydrase activity but no significant difference could be detected between actively boring and nonboring specimens. The possible involvement of these enzymes and their role in the mechanism of shell penetration by muricid gastropods has been discussed.

Intraspecific genetic variation of acid phosphatase activity in monokaryotic and dikaryotic populations of the ectomycorrhizal fungus Hebeloma cylindrosporum

1991 ◽  
Vol 69 (4) ◽  
pp. 808-813 ◽  
Author(s):  
J. P. Meysselle ◽  
G. Gay ◽  
J. C. Debaud
Keyword(s):  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Acid Phosphatase Activity ◽  
Specific Activity ◽  
Intraspecific Variability ◽  
Ectomycorrhizal Fungus ◽  
Hebeloma Cylindrosporum ◽  
Single Strain ◽  
Wild Strains

Intraspecific variability of acid phosphatase activity and mycelial growth of the ectomycorrhizal fungus Hebeloma cylindrosporum Romagnesi was examined because of the role of this enzyme activity in the phosphate nutrition of the fungus and consequently of mycorrhizal host plants. Interstrain variation was studied with 11 wild strains, and intrastrain variability was studied with 20 sib-monokaryons and 50 reconstituted dikaryons, progeny of the HC1 fruiting strain. The range of variation of acid phosphatase activity among wild dikaryotic mycelia was the same as that among sib-monokaryons or dikaryons belonging to the progeny of a single strain. The total phosphatase activity of the wild strains ranged from 5.70 to 96.0 total milliunits (TmU). It ranged from 11.1 to 120.5 TmU within sib-monokaryons and from 34.2 to 178.1 TmU for reconstituted dikaryons. Specific phosphatase activity of wild dikaryons ranged from 48.5 international milliunits (ImU) to 675.6 ImU, whereas the ranges of variation among sib-monokaryons and reconstituted dikaryons were, respectively, 85.3–791.0 and 270.7–816.1 ImU. On average, sib monokaryons and reconstituted dikaryons had lower activity than their parental dikaryon. However, four reconstituted dikaryons had a higher specific activity than the original dikaryon HC1. The growth of the studied mycelia also varied, but in a narrower range (from 97.1 to 151.6 μg protein per culture for wild dikaryons, from 130.1 to 199.1 μg for sib-monokaryons, and from 160.6 to 275.9 μg for reconstituted dikaryons). No correlation could be detected between specific acid phosphatase activity and growth rate in pure culture within the different monokaryotic or dikaryotic populations studied. These results demonstrate the possibility of obtaining, by intrastrain crossings, mycelia having higher phosphatase activity than the parental wild strains. The characteristics of the different mycelia are discussed in relation to a selection program and their putative spatial distribution in natural conditions. Key words: acid phosphatase, ectomycorrhizal fungus, intraspecific variation, monokaryon, dikaryon, Hebeloma cylindrosporum.

WEIGHT AND VOLUME CHANGES AND ACID PHOSPHATASE ACTIVITY OF THE CORPUS LUTEUM OF HYPOPHYSECTOMISED AND CAESARIAN SECTIONED PREGNANT RATS

1972 ◽  
Vol 70 (1) ◽  
pp. 156-162 ◽  
Author(s):  
H. B. Waynforth
Keyword(s):  
Acid Phosphatase ◽  
Corpus Luteum ◽  
Phosphatase Activity ◽  
Acid Phosphatase Activity ◽  
Free Acid ◽  
Caesarian Section ◽  
Pregnant Rats ◽  
Proportional Increase ◽  
Structural Regression

ABSTRACT Rats hypophysectomised on Day 8 of pregnancy showed no growth or involution of the corpus luteum four days later but there was a significant increase in the total and free acid phosphatase activities. Hypophysectomy on Day 12 did not affect the expected changes in luteal weight and acid phosphatase activity but did increase the volume of the corpus luteum on Day 16 compared to intact pregnant rats. Concurrently performed hypophysectomy and Caesarian section caused a greater rate of luteal regression and a greater increase in acid phosphatase activity than did Caesarian section alone. Although involution of the corpus luteum was progressively advanced by 32 days after the initiation of gestation in rats hypophysectomised or hypophysectomised plus Caesarian sectioned on Day 8 and 12 respectively, there was no proportional increase in the acid phosphatase activity. The role of acid phosphatase in the structural regression of the rat corpus luteum is considered to be minimal.

scholarly journals Amino Acid Phosphatase Activity of Alkaline Phosphatase. A Possible Role of Protein Phosphatase

1995 ◽  
Vol 227 (1-2) ◽  
pp. 367-371 ◽  
Author(s):  
Tetsuya Shinozaki ◽  
Hideomi Watanabe ◽  
Satoru Arita ◽  
Masaki Chigira
Keyword(s):  
Alkaline Phosphatase ◽  
Acid Phosphatase ◽  
Amino Acid ◽  
Phosphatase Activity ◽  
Protein Phosphatase ◽  
Acid Phosphatase Activity

Erythrophagocytosis in the Liver in Hemolytic Anemias

1968 ◽  
Vol 26 ◽  
pp. 184-185
Author(s):  
O. T. Minick ◽  
E. Orfei ◽  
F. Volini ◽  
G. Kent
Keyword(s):  
Acid Phosphatase ◽  
Oxidative Damage ◽  
Phosphatase Activity ◽  
Kupffer Cells ◽  
Acid Phosphatase Activity ◽  
Common Type ◽  
Red Cell ◽  
Cell Fragments ◽  
Reticulo Endothelial System ◽  
Important Site

Hemolytic anemias were produced in rats by administering phenylhydrazine or anti-erythrocytic (rooster) serum, the latter having agglutinin and hemolysin titers exceeding 1:1000.Following administration of phenylhydrazine, the erythrocytes undergo oxidative damage and are removed from the circulation by the cells of the reticulo-endothelial system, predominantly by the spleen. With increasing dosage or if animals are splenectomized, the Kupffer cells become an important site of sequestration and are greatly hypertrophied. Whole red cells are the most common type engulfed; they are broken down in digestive vacuoles, as shown by the presence of acid phosphatase activity (Fig. 1). Heinz body material and membranes persist longer than native hemoglobin. With larger doses of phenylhydrazine, erythrocytes undergo intravascular fragmentation, and the particles phagocytized are now mainly red cell fragments of varying sizes (Fig. 2).

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