• Title, Summary, Keyword: alkaline phosphatase

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Optimal Production of Thermostable Alkaline Phosphatase from Thermus caldophilus GK24 (Thermus caldophilus GK24로부터 내열성 alkaline phosphatase의 최적생산)

  • Kim, You-Jin;Chun, Myung-Sook;Kim, Hyun-Kyu;Kwon, Suk-Tae
    • Applied Biological Chemistry
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    • v.38 no.5
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    • pp.376-381
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    • 1995
  • Thermus caldophilus GK24 was selected as sources of thermostable alkaline phosphatase from a survey of extreme thermophile. T. caldophilus GK24 was tested for production of alkaline phosphatase by addition of various concentration of sodium glutamate, bactotryptone, glucose and yeast extract to basal salts. Sodium glutamate was found to be effective for the alkaline phosphatase induction. The optimal induction medium for production of alkaline phosphatase involves the addition of 0.3% sodium glutamate, 0.2% bactotryptone and 0.5% glucose to basal salts. The activity of the enzyme in optimal induction medium increased nearly 6-fold/ml than basal medium and 27.5-fold/ml than standard medium. T. caldophilus GK24 alkaline phosphatase was found to be inducible. When starved of inorganic phosphate, T. caldophilus GK24 produces the enzyme alkaline phosphatase. The addition of inorganic phosphate to growth medium had a repressive effect on enzyme synthesis.

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A Study on the Alkaline Phosphatase Activity in the Digestive Tracts of Fishes (魚類消化管의 Alkaline Phosphatase 活性에 관한 硏究)

  • 하재청;김국찬
    • The Korean Journal of Zoology
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    • v.17 no.4
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    • pp.167-176
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    • 1974
  • The authors have studied the distribution of alkaline phosphatase in the pharynx, esophagus, stomach (or intestinal bulb), anterior and posterior portions of intestine of three kinds of fishes. The results obtained are as follows: 1. Alkaline phosphatase activity of basal cells in the pharyngeal epithelium of loach and snakehead fish showed moderately positive reaction, and basal cells in the esophagel epithelium of loach and eel showed also moderately positive reaction. 2. Goblet cells of pharynx, esophagus, intestinal bulb and intestinal mucosa, and gastric glandular cells of the above fishes showed negative reaction for alkaline phosphatase. 3. Strongly positive reaction for alkaline phosphatase was observed at both intestinal bulb and the free border of intestinal epithelium, but weak positive reaction at the free border of posterior portion of loach intestine.

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Alkaline Phosphatase Activity in the Developing Pronephros and Mesonephros of the Frog Bombina orientalis (발생중의 무당개구리 前賢 및 中賢의 Alkaline Phosphatase활성)

  • Jae Chung Hah
    • The Korean Journal of Zoology
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    • v.17 no.4
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    • pp.177-184
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    • 1974
  • The cobalt capture method of Gomori's modified technique(Gomori, 1952) was employed to study the histochemistry of the developing frog kidney. Alkaline phosphatase activity was observed in association with the brush borders of pronephros and mesonephros. By the stage of transition from larva to tadpole alkaline phosphatase activity was gradually increased in the brush border of pronephros, and as the pronephros begun to degenerate the enzyme activity was decreased and disappeared. By the time of maximum development of the pronephros the mesonephros began to develop and alkaline phosphatase activity of the mesonephric tubules showed highly positive throughout the stage of metamorphosis. No activity was observed in association with the collecting tubules and ductal elements.

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Characteristics of Alkaline and Acid Phosphatase in Echinostoma hortense (호르텐스극구흡충에서 Alkaline Phosphatase 및 Acid Phosphatase의 특성)

  • 양용석;김인식;임지애;강성구;박주연
    • Biomedical Science Letters
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    • v.5 no.1
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    • pp.119-129
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    • 1999
  • This study was aimed to investigate the enzyme-histochemical localization and characteristics of alkaline and acid phosphatase extracted from adult of Echinostoma hortense. Using the Gomori calcium stain and the Gomori lead nitrate satin method, we found that the alkaline and acid phosphatases were localized mostly in the intestine, vitellaria and pharynx of Echinostoma hortense. The three isozymes of alkaline phosphatase and two isozymes of acid phosphatase were separated from Echinostoma hortense by electrophoresis. The isozymes of alkaline phosphatase were 145.9, 207.5, 220.8 kDa and the isozymes of acid phosphatase were 179.5 and 209.4 kDa. The activity of alkaline phosphatase was denatured completely after heating at 9$0^{\circ}C$ for 12 seconds. The optimum pH and temperature for activity of alkaline phosphatase were about pH 9 and 4$0^{\circ}C$, while the optimum pH for activity of acid phosphatase was about pH 5. The maximum activity of alkaline phosphatase was at 189 unit, but maximum activity of acid phosphatase was at 71 unit As the result from above, we observed that alkaline and acid phosphatases funtion mainly in the alimentary tract and vitellaria. Echinostoma hortense performs the parasitism in the intestine of host by using proper isozyme of phosphatase.

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The effects of continuous and intermittent compressive pressure on alkaline phosphatase activity of MC3T3-E1 cells (지속적 및 간혈적 가압력이 MC3T3-E1 세포의 Alkaline phosphatase 활성도에 미치는 영향)

  • Song, Hye-Seob;Kyung, Hee-Moon
    • The korean journal of orthodontics
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    • v.26 no.4
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    • pp.449-454
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    • 1996
  • The propose of this study was to evaluate the difference of cellular activity dependent on intermittent compressive force by determining the alkaline phosphatase activity. Alkaline phosphatase activity was measured on control and experimental groups every 24, 48, 72hours. Experimental groups consisted of continous and intermittent compressive group which were compressed by $300gm/cm^2$ of diaphram pump. The intermittent compressive group was connected by timer which was worked on 10 minutes an off 10 minutes. The results were as follows; 1. The alkaline phosphatase activity between control and experimental groups showed not significant difference at compressed 24 hours. 2. The alkaline phosphatase activity of experimental groups were more increased than control group at compressed 48 hours. 3. The alkaline phosphatase activity of intermittent compressive group showed significant increased to control group. Whereby continuous compressive group showed not significant difference to control at 72 hours. 4. The alkaline phosphatase activity of intermittent compressive group were stringly increased than continuous compressive groups. 5. Between experimental groups and control group no other morphologic changes were detected by microscopic findings.

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Studies on the Alkaline Phosphatase of Pekin Duck: I. Some Properties of Liver Alkaline Phosphatase

  • Kang, Shin-Sung;Park, Tae-Kyu
    • The Korean Journal of Zoology
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    • v.25 no.2
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    • pp.71-80
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    • 1982
  • Some properties of alkaline phosphatase, partially purified from the liver of the local Pekin duck, Anas platyrhynchos, were investigated with the following results. 1. Gel-filtration of the duck liver extract indicated the presence of two molecular-weight species of alkaline phosphatase. 2. Electrophoresis of both enzyme preparations suggests the presence of two molecular forms of alkaline phosphatase with different physicochemical characteristics. 3. The liver alkaline phosphatase has an optimum pH of 9.0, and is further activated by $Mg^2+$ but not by $Ca^2+$. 4. The enzyme was relatively heat-labile, and was competitively inhibited by phosphate ions, but uncompetitively inhibited by L-phenylalanine. 5. These results are discussed in comparison with the properties of human and other animal alkaline phosphatases.

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Changes in Phosphatase Activity of the Mouse Uterus during the Estrous Cycle (發情週期에 EK른 생쥐子宮의 Phosphatase 活性의 變化에 관하여)

  • Kim, Moon-Kyoo;Kim, Sung-Rye;Cho, Wan-Kyoo
    • The Korean Journal of Zoology
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    • v.23 no.2
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    • pp.61-68
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    • 1980
  • Quantitative analysis of the activities of transport ATPases as well as alkaline phosphatase of the mouse uterus was carried out during the estrous cycle. Even though the proportional patterns of the enzyme activities were similar each another between the stages of estrous cycle, the absolute activities of the enzymes except $K^+$-dependent and $Na^+$, $K^+$-activated ATPases at the time of estrus were significantly (p<0.025) higher than that at any other time of the estrous cycle. That is, the activities of $K^+$-dependent and $Na^+$, $K^+$-activated ATPases were negligible during the period of time from diestrus to estrus while the little activities (0.04 $\\sim$ 0.05$\\mu$M/mg protein/hr in average, $6\\sim7$% of the total enzyme activity) of these enzymes appeared at the time of metaestrus. On the other hand, at the time of estrus, the activities of $Mg^++$-dependent phosphatase, transport ATPase and alkaline phosphatase were rapidly and tremendously increased to be 0.69 (35%), 0.42 (21%) and 1.58 (79%), respectively. The activity of alkaline phosphatase was in the range of 0.60 $\\sim$ 1.58 (79 $\\sim$ 90%) and predominant throughout the estrous cycle. The activity of $Mg^++$-dependent alkaline phosphatase was estimated as 12 $\\sim$ 16% of the total enzyme activity. Therefore, it is assumed likely that $K^+$-dependent and $Na^+$, $K^+$-activated ATPases are not the main factors to control the fluid accumulation at the time of estrus, but may be the factors to reabsorb the luminal fluid into the uterine epithelium at the time of metaestrus, and that $Mg^++$-dependent phosphatase, transport ATPase and alkaline phosphatase must be closely involved in the secretion of luminal fluid from the epithelial cells of the mouse uterus.

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Inorganic Phosphate Has the Inhibitory Effect on Phosphotyrosyl Phosphatase Activity of Alkaline Phosphatase in Rabbit Plasma (인산에 의한 토끼 혈장 Alkaline Phosphatase의 Phosphotyrosyl Phosphatase 활성 저해)

  • Lee, Kyung Tae;Seo, Soong Hoon;Kim, Dong Hyun
    • Korean Journal of Clinical Pharmacy
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    • v.9 no.1
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    • pp.62-65
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    • 1999
  • Inorganic phosphate (Pi) in rabbit plasma was found to block completely phosphotyrosine phosphatase (PTPase) activity without affecting the alkaline phosphatase (ALPase) activity. Our results provided that (1) PTPase activity and inhibitor are separated after G-25 gel-filtration. (2) This inhibitor is heat stable and trypsin-resistant and it can be removed by dialysis using 3 Kd cut-off tubing. (3) The elution pattern of the inhibitor is identical to that of Pi, and by performing a seperate run with inorganic phosphate. (4) The PTPase activity was recovered following an incubation with $CaCl_2$ (10 mM).

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Alkaline Phosphatase Activity and Phosphatase Hydrolyzable Phosphorus for Phytoplankton in Hiroshima Bay, Japan

  • Oh, Seok-Jin;Yoon, Yang-Ho;Yamamoto, Tamiji;Matsuyama, Yukihiko
    • Ocean Science Journal
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    • v.40 no.4
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    • pp.183-190
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    • 2005
  • We investigated the seasonal variability of tree alkaline phosphatase activity in seawater and alkaline phosphatase hydrolysable phosphorus (APHP) at 3 stations in Hiroshima Bay using alkaline phosphatase extracted from the dinoflagellates Alexandrium tamarense and Gymnodinium catenatum. The dissolved inorganic phosphorus (DIP) was lower than $1\;{\mu}M$ all samples; the lowest values were in May. The amount of APHP was high at the surface and bottom waters of all stations in May, showing DIP-depleted conditions. In August and November, the amount of APHP was much less than the amount of APHP in May, indicating that the availability of dissolved organic phosphorus (DOP) for these species was low and/or uptake during the dinoflagellate blooming might have occurred in the area. The results obtained from short-term variations of AP activity might suggest that the growth of dinoflagellates in this season may be partly supported by the AP produced by other diatoms.

Activity of Alkaline Phosphatase from the Mosquito, Culex pipiens pallens (홍모기(Culex pipiens pallens)의 난성숙 과정 중 alkaline phosphase의 활성)

  • 이영수;이승훈;박영민;성기창
    • The Korean Journal of Zoology
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    • v.36 no.3
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    • pp.425-432
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    • 1993
  • Alkaline phosphatase from Culex pipiens pallens was examined to determine the optimal assay condition and to assay the activity during ovarian development. The activity of alkaline phosphatase in a male and a nongravid female continuously were declined after eclosion. But by the stimulus of a blood meal, the enzyme activity was increased dramatically. At 30 hr. after a blood meal, the maximal activity was reached and then declined. And after 48 hr. after a blood meal, the second activity increase was revealed. This second increase was maintained up to oviposition. The first activity increase was revealed in the midgut and the second increase was done in the ovary to assay the organ distribution of alkaline phosphatase. In electrophresis data, it was shown 5 isozyme bands, ALP-1 and ALP-2 in the ovary, ALP-3 in the thorax and the midgut, and ALP-4 and ALP-5 in the thorax, the fatbody and the midgut in crude extract at 30 hr. after a blood meal. One the same ovary pattern were shown at 72 hr. after a blood meal.

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