Acid phosphatase in eggs of the zebrafish,Brachydanio rerio

Summary 2 isozymes of acid phosphatase have been identified by polyacrylamide disc gel electrophoresis in the ovary and mature, unfertilized eggs ofB. rerio. Histochemically, the enzyme appears to be localized in preyolk bodies of previtellogenic oocytes and in yolk platelets of vitellogenic and postvitellogenic oocytes. The contents of the cortical granules at all stages of oocyte differentiation were acid phosphatase negative.     

Über DPNH-Diaphorase und alkalische Phosphatase bei Präimplantationsstadien des Goldhamsters (Mesocricetus auratus Waterh.)

Summary The activity of the DPNH-diaphorase and the alkaline phosphatase were examined in golden-hamster eggs prior to fixation. The reactions for DPNH-diaphorase as well as for alkaline phosphatase were found to be positive already in the undivided egg and in early cleavage stages. The reaction products of both enzyme determinations showed a histophotometrically measurable polar distribution in the cytoplasm, in the one-cell stage as well as in the individual blastomeres of the examined early cleavage stages.     

Enzymhistochemische Untersuchungen an durstaktivierten neurosekretorischen Zellen der Ratte

Summary In hypothalamic neurosecretory nuclei of rats subject to water withdrawl for 1–14 days, a marked increase in the activities of histochemically detected acid phosphatase, thiamine pyrophosphatase and glucose-6-phosphate dehydrogenase is observed. LDH and SDH activities do not change. Two different cell types can be distinguished by means of the acid phosphatase and TPPase reactions.     

Zytologische Untersuchungen an der Reblaus-Blattgalle

Summary Up to 9 types of cell nuclei, distinguished by their size, were found in the tissue of galls, which are produced by the vine louse. The growth of the cell nuclei probably proceeds in a series of prophase-like intermediate stages from one type of nuclei size to the next largest by means of endomitotic or endomitosis-like processes.     

Differential expression of monomeric and proteolytically processed forms of tartrate-resistant acid phosphatase in rat tissues

Purple acid phosphatase (PAP), also known as tartrate-resistant acid phosphatase (TRAP), uteroferrin or type 5 acid phosphatase (Acp5) is synthesized as an N-glycosylated monomeric latent precursor, which can be processed by limited proteolysis to a disulfide-linked two-subunit form with increased enzyme activity. In this study, we disclosed that the proteolytically processed two-subunit form constitutes the major PAP/TRAP variant in monocytic cells in spleen, thymus, liver and colon. In addition significant expression of the monomeric PAP/TRAP, indicating a non-enzymatic function, was detected in epithelial cells of colon, lung and kidney. Interestingly, proteolytic processing alone did not activate the enzyme but rendered the enzyme more susceptible to activation by reductants. Thus, beside limited proteolysis, the subcellular redox state could also be a determinant of enzyme action in vivo. The co-localization of PAP/TRAP and the cysteine protease cathepsin L could suggest a role for cathepsin L in the in vivo proteolytic processing of PAP/TRAP in monocytic cells.Received 10 December 2004; received after revision 19 January 2005; accepted 9 February 2005     

La phosphatase des os et le mécanisme général de l'ossification

Summary A general survey of the actual knowledges on the bone phosphatase is given. The enzyme plays an important rôle in the calcification of bone and teeth, this process being unable to proceed at a physiological speed without the participation of a phosphatase. The biological function of the enzyme is thus to accelerate and not to promote the calcification.The knowledge of the mechanism of phosphatase activity in the skeletal organs and of the chemical composition of the bone salt cannot lead to a full understanding of the physiology of ossification. A prominent function in this field is devoted to the proteins of the ground substance of bone and to their evolution. The study of the protein matrix of bone is now the most important subject of work for the biochemistry of ossification.

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Conférence faite le 28 mai 1946 au Hallerianum de l'Université de Berne.     

Partial purification and characterization of acid phosphatase from sporulated oocysts ofEimeria tenella

Summary Acid phosphatase ofEimeria tenella oocysts (Peak II) was purified 77-fold with a recovery of 26% using protamine sulfate precipitation, DEAE-cellulose chromatography and Sephadex G-200 gel filtration. This enzyme occurs in multiple forms as indicated by two peaks which can be separated by DEAE-cellulose chromatography and polyacrylamide gel electrophoresis. The partially purified enzyme has optimal activity at pH 4.5. With p-nitrophenyl phosphate the Km and V_max values for (Peak II) were 25 mM and 1.57 mol/min/mg protein, respectively. The enzyme (Peak II) ist strongly inhibited by Hg⁺⁺, Cu⁺⁺, iodoacetamide, fluoride and molybdate. Tartrate and other divalent metal ions have no effect on enzyme activity. The partially purified Peak II phosphatase is not a glycoprotein as it is not absorbed on concanavalin-A Sepharose and its treatment with bacterial neuraminidase does not alter its elution profile through DEAE cellulose.     

Phosphomonoesterases in the 2 sexes of the root-knot nematode,Meloidogyne lucknowica Singh, 1969

Summary The 2 phosphomonoesterases of the root-knot nematode were colorimetrically determined. Alkaline phosphatase activity was observed to be lower than the acid phosphatase activity. Sex related trends were clearly seen in the enzyme levels of the 2 sexes of thenematode. Alkaline phosphatase level differed 28.76%, while acid phosphatase level differed 60.36% in the 2 sexes.The authors are grateful to the Council of Science and Technology U.P. for the grant of a Research Scheme for these studies.     

Fermenthistochemische Untersuchungen am Übergangsepithel verschiedener Säugetiere

Summary Histochemical investigations on enzyme activities in the transitional epithelium showed positive reactions with succinic dehydrogenase, esterase, alkaline phosphatase, acid phosphatase and amylophosphorylase (incl. branching factor). Negative results were drawn from cholinesterase, 5-nucleotidase, glucose-6-phosphatase, and carbonic anhydrase.

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Mit dankenswerter Unterstützung durch die Deutsche Forschungsgemeinschaft.     

Acid phosphatase activity of small intestine of mice after exposure to different doses of gamma rays

Summary Effect of whole-body radiation at 3 different dose levels on the activity of acid phosphatase was studied in the small intestine of Swiss albino mice. In all the 3 exposure groups the enzyme activity increased significantly at 24 h after irradiation; the time at which the maximum histological damage was seen. With the beginning of recovery the enzyme tended to decrease and gradually approached control values.