• 미생물학회지
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• 제23권3호
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• pp.172-176
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• 1985

본 연구는 효모세포 (Saccharomyces uvarum)의 ACPase, ALPase의 Isoenzyme type을 규명함과 아울러, iso-enzyme type중 어느 것이 constituitive 또는 repressible enzyme type인가를 조사하고, 각각의 isoenzyme활성도 비율을 살펴보아 배양조건(catabolic repression and derepression) 및 무기인산 제한에 따른 각 type의 세포내 조절기능을 분석하고자 하였다. Acid phosphatase는 또 다른 isoenzyme type이 발견되지 않았으나, alkaline phosphatase의 경우는 3가지 type이 p-NPP에 specificity를 지녔다. 세포질의 수용성단백질 분석결과 exponential phase의 세포는 주로 음전하를 띤 단백질이 높은 함량을 나타내었다. 당과 인산이 결핍된 배지에서 생육권(catabolic repression)세포에서 AL P Pase isoenzyme 중 type “B"의 활성도가 매우 높아졌으나, 완전배지에서 배양된 (catabolic derepression)세포에서는 type “B"의 활성도 감소 및 type “C"의 활성도 증가 현상을 볼 수 있었다. ALPase 중 “A" peak는 constituitive enzyme, “B" peak는 repressible enzyme, peak “C"는 L-histidinol phosphatase로 추정되었다.

• 한국식품영양과학회지
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• 제23권3호
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• pp.490-495
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• 1994

Acid phosphatase (EC3.1.3.2) from carrots was partially purified by ammonium sulfate fractionation (30%-80%), Sephacryl S-200 gel filtration, cm-Sepharose CL-6B and DEAE -Sephacel ion exchange chromatography. The optimum ph and temperature of acid phosphatase from carrots were pH 5.5 and 55$^{\circ}C$, respectively. The enzyme was most stable at ph 6.0 and relatively unstable below pH 4.0 . The activation energy of the enayme was determined to be 10.6kcal/mole. The enzyme utilized p-nitrophenyl phosphate as a substrate among tested possible substrates, whereas it hydrolyzed 5' -IMP and 5'-GMP poorly. The Michaelis -Menten constant(Km) of the enzyme with p-nitrophenyl phosphate as a substrate was identified as 0.55mM. Amongtested metal ions and inhibitors, Al+++ Zn++, Cu++ , fluoride, metavanadate and molybdate ions inhibited the enzyme activity drastically.

• Journal of Plant Biology
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• 제21권1_4호
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• pp.39-44
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• 1978

Acid phosphatase activities were analyzed in $\mu\textrm{g}$ tissue samples from an angiosperm parasite (Cuscuta cephalanthi) and its host plant (Hedera helix) by a fluorometric microtechnique. The apex and the coiling portion of the parasite axis exhibited greater enzyme activies than other portions of the hypha. Acid phosphatase activity in the haustorium was 2-3 times that in the hyphal axis. The vascular bundles of the normal host exhibited the greatest enzyme activity. The acid phosphatase activity in the host infected by the parasite decreased to the activity level of the haustorium.

• 한국동물학회지
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• 제16권2호
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• pp.139-145
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• 1973

솔나방(Dendrolimus spectabilis)의 變態에 따른 acid 및 alkaline phosphatase의 活性度의 變化를 測定하였다. 두 酵素의 活性度는 幼蟲의 成長과 더불어 增加하고 전용기에서 減少하였다. Acid phosphatase는 용기의 初에, 그리고 alkaline phosphatase는 幼蟲8齡에서 각각 最高의 活性을 나타내었다. 전용기에서 두 酵素간의 活性度의 차이는 크게 나타나지 않았으나 幼蟲8齡에서 보다는 훨씬 낮았다. Acid phosphatase의 活性度는 용기초에 增加하고 용기말에서 減少하다가 成蟲에서 다시 上昇하였다. Total phosphatase의 活性度의 變化는 變態에 따른 生理的曲線인 U字型 pattern을 나타내었다.

• 한국식품과학회지
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• 제28권4호
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• pp.663-667
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• 1996

파로부터 acid phosphatase를 Sephacryl S-200 gel filtration과 CM-Sepharose CL-6B ion exchange chromatography를 이용하여 부분정제하였다. p-nitrophenyl phosphate를 기질로 사용했을 경우에 최적pH는 5.5, 최적온도는 $60^{\circ}C$였다. 효소의 활성화 에너지는 4.86kcal/mole이었다. 효소는 pH 6.0에서 가장 안정하였으며, $50^{\circ}C$ 이하에서 대체로 안정하였다. 효소는 p-nitrophenyl phosphate를 기질로 가장 잘 이용하였으며, 5'-IMP와 5'-GMP는 기질로 거의 이용하지 못하였다. 효소는 p-nitrophenyl phosphate를 기질로 했을 경우에 $K_{m.app.}$값이 0.87mM이었다 $Cr^{+++},\;Zn^{++},\;Cu^{++}$이온은 효소의 활성을 저해하였으며, 또한 molybdate와 metavanadate 이온이 효소의 활성을 저해하였다. 그리고, NaCl의 농도가 높을수록 효소의 활성을 저해하였다.

• Journal of Plant Biology
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• 제21권1_4호
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• pp.13-21
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• 1978

The effect of cyclic-AMP on the induction of acid phosphatase activity in barley aleurone layers was examined. Tannic acid was used as a inhibitor. Decursinol and coumarin were also used as a comparison. Maxiumu promotion of the enzyme activity was obtained with 10-5M cyclic-AMP, but this promotion was lower than that of 10-5M GAS induced enzyme activity in incubation medium. The inhibition rate in the addition of tannic acid was shown 17% and 63% at a ratio to GAs (by weight) of 10 : 1, and 58% and 94% at a ratio of 100 : 1 treated with GAs, and cyclic-AMP, respectively. The most potentiation of 10-6M GAS effect was induced by the additiion of suboptimal concentration (10-6M) of cyclic-AMP. Additional GAs and cyclic-AMP were shown the recovery of the enzyme activity inhibited by tannic acid. The combination with cyclic-AMP and theophylline enhanced the enzyme activity, too. Any other nucleotides tested except cyclic-AMP didn't show the action. There were no differences in acid phosphatase isozyme patterns by polyacrylamide disc electrophoresis, in conjunction with the different additions but the size of bands showed great differences. Especially, the 3rd band and the 5th band group were remarkable.

• 한국환경보건학회지
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• 제17권2호
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• pp.121-126
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• 1991

To clarify a cause of increased serum level of acid phosphatase in CCl$_{4}$-treated rats, the acid phosphatase activity of liver was compared with that serum. Concomitantly, the serum and liver acid phosphatase activity of CCl$_{4}$-treated rats were compared with that of CCl$_{4}$-treated rats pretreated with prednisolone or actinomycin D. In CCl$_{4}$-treated rats, the activity of serum acid phosphatase was significiantly increased whereas that of liver acid phosphatase was rather slightly decreased. the pretreatment of prednisolone led to the decreased activity of serum and liver acid phosphatase in CCl$_{4}$-treated rats. But the pretreatment of actinomycin D rather increased the activity of liver and serum enzyme. In conclusion, it is likely the increased activity of serum acid phosphatase is based on the excess leaking of acid phosphatase into blood by the increased membrane permeability of both liver cell and lysosome in it.

• Parasites, Hosts and Diseases
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• 제31권2호
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• pp.165-168
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• 1993

서울주걱흡충의 냉동절편에서 효소조직화학법을 이용하여 조직융해구(trlbocytic organ)와 맹장에 acid phosphatase, non-specific esterase 활성도가 있음을 알 수 있었다. 이 두 기관이 표피 이외에 중요한 흡수기관일 것이다. 이 흡충의 우리말 이름을, 이미 회원들에 의해 제안된 "쥐주걱흉충"은 쥐만 적절한 숙주로 생각할 수 있으므로 발견 장소가 학명에 포함된 것을 감안하여 "서울주걱흡충"이라고 고쳐 쓰고 싶다. 준말로 쓸 때는 "서울흡충"이 나을 것이다.

• 한국미생물·생명공학회지
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• 제25권3호
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• pp.271-276
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• 1997

An ascorbic acid phosphorylating enzyme, which catalyzes the formation of ascorbic acid-2-phosphate from ascorbic acid and pyrophosphate, was purified 32.7-folds to homogeneity from a cell-free extract of Cellulomonas sp. AP-7. The combination of DEAE- Sephacel ion exchange chromatography and Sephacryl S-200 get filtration was used for their purification. The molecular weight of the native protein was estimated to be 96.lkDa on high performance gel filtration chromatography. The SDS-PAGE analysis indicated that the protein consisted of four identical subunits of 24.6 kDa. The purified enzyme showed the optimal tempeature of 40$\circ$C and optimal pH of 4.5. The Km for ascorbic acid and pyrophosphate were 119 mM and 11.9 mM, respectively. The addition of 5,5'-dithiobis-(2-nitrobenzoic acid) into the reaction mixture resulted in the reduction of the enzyme activity at 51%. The enzyme also had a phosphatase activity at weakly acidic pH and the Km for ascorbic acid-2-phosphate in phosphatase activity was 7.9 mM.

• Journal of Microbiology and Biotechnology
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• 제21권5호
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• pp.483-493
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• 2011

An acid phosphatase (HppA) activated by $NH_4Cl$ was purified 192- and 34-fold from the periplasmic and membrane fractions of Helicobacter pylori, respectively. SDS-polyacrylamide gel electrophoresis revealed that HppA from the latter appears to be several kilodaltons larger in molecular mass than from the former by about 24 kDa. Under acidic conditions (pH${\leq}$4.5), the enzyme activity was entirely dependent on the presence of certain mono- and/or divalent metal cations (e.g., $K^+$,$ NH_4{^+}$, and/or $Ni^{2+}$). In particular, $Ni^{2+}$ appeared to lower the enzyme's $K_m$ for the substrates, without changing $V_{max}$. The purified enzyme showed differential specificity against nucleotide substrates with pH; for example, the enzyme hydrolyzed adenosine nucleotides more rapidly at pH 5.5 than at pH 6.0, and vice versa for CTP or TTP. Analyses of the enzyme's N-terminal sequence and of an $HppA^-$ H. pylori mutant revealed that the purified enzyme is identical to rHppA, a cloned H. pylori class C acid phosphatase, and shown to be the sole bacterial 5'-nucleotidase uniquely activated by $NH_4Cl$. In contrast to wild type, $HppA^-$ H. pylori cells grew more slowly. Strikingly, they imported $Mg^{2+}$ at a markedly lowered rate, but assimilated urea rapidly, with a subsequent increase in extracellular pH. Moreover, mutant cells were much more sensitive to extracellular potassium ions, as well as to metronidazole, omeprazole, or thiophenol, with considerably lowered MIC values, than wild-type cells. From these data, we suggest that the role of the acid phosphatase HppA in H. pylori may extend beyond 5'-nucleotidase function to include cation-flux as well as pH regulation on the cell envelope.