Mandić, Ljuba M.

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Isolation and partial characterization of an acid phosphatase from Artemisia vulgaris pollen extract

Ćirković-Veličković, Tanja; Gavrović-Jankulović, Marija; Bukilica, Mirjana; Mandić, Ljuba M.; Petrović, Spomenka; Jankov, Ratko

(Srpsko hemijsko društvo, Beograd, 2002)

TY  - JOUR
AU  - Ćirković-Veličković, Tanja
AU  - Gavrović-Jankulović, Marija
AU  - Bukilica, Mirjana
AU  - Mandić, Ljuba M.
AU  - Petrović, Spomenka
AU  - Jankov, Ratko
PY  - 2002
UR  - http://intor.torlakinstitut.com/handle/123456789/140
AB  - An acid phosphatase from an extract of mugwort (Artemisia vulgaris) pollen was purified by a factor of 48 by a combination of ion exchange and gel-chromatography. The molecular weights of the enzyme were 76 kDa and 73 kDa, determined by gel filtration on a Sephadex G-100 sf column and by SDS PAGE(under reducing and non-reducing conditions), respectively. In analytical isoelectrofocusing, the enzyme appears as two very close bands pI at about 4.2. The optimum pH for the enzyme is 5.4. The apparent Km for p-nitrophenyl phosphate was estimated to be 0.16mM. The purified enzyme has broad specificity, and hydrolyses p-nitrophenyl phosphate and α-naphthyl phosphate. Pyrophosphate and O-phospho-L-tyrosine were estimated to be the best substrates for this enzyme as potential in vivo substrates. The enzyme is inhibited competitively by phosphate (Ki = 1.25 mM), molybdate (Ki = 0.055 mM) and pyrophosphate (Ki = 6.7 mM) and non-competitively by fluoride (Ki = 9.8 mM). Metal ions such as Hg2+, Cu2+ and Zn2+ express an inhibitory effect on the enzyme, while the enzyme is slightly activated by non-ionic detergents, Tween 20 and Triton X-100. There is no change in the enzyme activity in the presence of tartrate, citrate, EDTA, 1,10-phenanthroline and sulfhydryl-group modifiers such as p-chloromercuribenzoate and N-ethylmaleimide.
AB  - Kisela fosfataza ekstrakta polena visokog korova (Artemisia vulgaris) je prečišćena 48 puta kombinacijom jonoizmenjivačke i gel-hromatografije. Molekulska težina enzima je 76 kDa i 73 kDa, određena gel-filtracijom na matriksu Sephadex G-100 sf i SDS PAG elektroforezom (pri redukujućim i neredukujućim uslovima), respektivno. Pri izoelektrofokusiranju, enzim se sastoji iz dve vrlo bliske trake pI vrednosti oko 4,2. Optimalno pH za aktivnost enzima je 5,4. PrividnoKmza hidrolizu p-nitrofenil-fosfata je procenjeno da je 0,16 mM. Prečišćeni enzim ima široku specifičnost hidrolizuje p-nitrofenil-fosfat i α-naftil-fosfat. Pirofosfat i O-fosfo-L-tirozin su procenjeni kao najbolji od potencijalnih in vivo supstrata ovog enzima. Enzim je inhibiran kompetitivno fosfatom (Ki=1,25 mM), molibdatom (Ki=0,055 mM) i pirofosfatom (Ki=6,7 mM) a nekompetitivno fluoridom (Ki= 9,8mM). Joni metala, kao što su Hg2+, Cu2+ i Zn2+ iskazuju inhibitorni efekat na enzim, dok je efekat ne-jonskih detergenata, kao što su Tween 20 i Triton X-100 blago aktivirajuć i. Nema promene u aktivnosti enzima u prisustvu tartarata, citrata, EDTA 1,10-fenantrolina i modifikatora sulfhidrilnih grupa kao što su p-hloromerkuribenzoat i N-etilmaleimid.
PB  - Srpsko hemijsko društvo, Beograd
T2  - Journal of the Serbian Chemical Society
T1  - Isolation and partial characterization of an acid phosphatase from Artemisia vulgaris pollen extract
T1  - Izolovanje i delimična karakterizacija kisele fosfataze ekstrakta polena Artemisia vulgaris
EP  - 572
IS  - 8-9
SP  - 567
VL  - 67
UR  - conv_17
ER  - 
@article{
author = "Ćirković-Veličković, Tanja and Gavrović-Jankulović, Marija and Bukilica, Mirjana and Mandić, Ljuba M. and Petrović, Spomenka and Jankov, Ratko",
year = "2002",
abstract = "An acid phosphatase from an extract of mugwort (Artemisia vulgaris) pollen was purified by a factor of 48 by a combination of ion exchange and gel-chromatography. The molecular weights of the enzyme were 76 kDa and 73 kDa, determined by gel filtration on a Sephadex G-100 sf column and by SDS PAGE(under reducing and non-reducing conditions), respectively. In analytical isoelectrofocusing, the enzyme appears as two very close bands pI at about 4.2. The optimum pH for the enzyme is 5.4. The apparent Km for p-nitrophenyl phosphate was estimated to be 0.16mM. The purified enzyme has broad specificity, and hydrolyses p-nitrophenyl phosphate and α-naphthyl phosphate. Pyrophosphate and O-phospho-L-tyrosine were estimated to be the best substrates for this enzyme as potential in vivo substrates. The enzyme is inhibited competitively by phosphate (Ki = 1.25 mM), molybdate (Ki = 0.055 mM) and pyrophosphate (Ki = 6.7 mM) and non-competitively by fluoride (Ki = 9.8 mM). Metal ions such as Hg2+, Cu2+ and Zn2+ express an inhibitory effect on the enzyme, while the enzyme is slightly activated by non-ionic detergents, Tween 20 and Triton X-100. There is no change in the enzyme activity in the presence of tartrate, citrate, EDTA, 1,10-phenanthroline and sulfhydryl-group modifiers such as p-chloromercuribenzoate and N-ethylmaleimide., Kisela fosfataza ekstrakta polena visokog korova (Artemisia vulgaris) je prečišćena 48 puta kombinacijom jonoizmenjivačke i gel-hromatografije. Molekulska težina enzima je 76 kDa i 73 kDa, određena gel-filtracijom na matriksu Sephadex G-100 sf i SDS PAG elektroforezom (pri redukujućim i neredukujućim uslovima), respektivno. Pri izoelektrofokusiranju, enzim se sastoji iz dve vrlo bliske trake pI vrednosti oko 4,2. Optimalno pH za aktivnost enzima je 5,4. PrividnoKmza hidrolizu p-nitrofenil-fosfata je procenjeno da je 0,16 mM. Prečišćeni enzim ima široku specifičnost hidrolizuje p-nitrofenil-fosfat i α-naftil-fosfat. Pirofosfat i O-fosfo-L-tirozin su procenjeni kao najbolji od potencijalnih in vivo supstrata ovog enzima. Enzim je inhibiran kompetitivno fosfatom (Ki=1,25 mM), molibdatom (Ki=0,055 mM) i pirofosfatom (Ki=6,7 mM) a nekompetitivno fluoridom (Ki= 9,8mM). Joni metala, kao što su Hg2+, Cu2+ i Zn2+ iskazuju inhibitorni efekat na enzim, dok je efekat ne-jonskih detergenata, kao što su Tween 20 i Triton X-100 blago aktivirajuć i. Nema promene u aktivnosti enzima u prisustvu tartarata, citrata, EDTA 1,10-fenantrolina i modifikatora sulfhidrilnih grupa kao što su p-hloromerkuribenzoat i N-etilmaleimid.",
publisher = "Srpsko hemijsko društvo, Beograd",
journal = "Journal of the Serbian Chemical Society",
title = "Isolation and partial characterization of an acid phosphatase from Artemisia vulgaris pollen extract, Izolovanje i delimična karakterizacija kisele fosfataze ekstrakta polena Artemisia vulgaris",
pages = "572-567",
number = "8-9",
volume = "67",
url = "conv_17"
}
Ćirković-Veličković, T., Gavrović-Jankulović, M., Bukilica, M., Mandić, L. M., Petrović, S.,& Jankov, R.. (2002). Isolation and partial characterization of an acid phosphatase from Artemisia vulgaris pollen extract. in Journal of the Serbian Chemical Society
Srpsko hemijsko društvo, Beograd., 67(8-9), 567-572.
conv_17
Ćirković-Veličković T, Gavrović-Jankulović M, Bukilica M, Mandić LM, Petrović S, Jankov R. Isolation and partial characterization of an acid phosphatase from Artemisia vulgaris pollen extract. in Journal of the Serbian Chemical Society. 2002;67(8-9):567-572.
conv_17 .
Ćirković-Veličković, Tanja, Gavrović-Jankulović, Marija, Bukilica, Mirjana, Mandić, Ljuba M., Petrović, Spomenka, Jankov, Ratko, "Isolation and partial characterization of an acid phosphatase from Artemisia vulgaris pollen extract" in Journal of the Serbian Chemical Society, 67, no. 8-9 (2002):567-572,
conv_17 .