Enzymatic Characterization of Acid Phosphatase in the Logarithmic and Stationary Phase of Leishmania major Promastigotes

2015 ◽  
Vol 16 (1) ◽  
Author(s):  
Amir Navabi ◽  
Simindokht Soleimanifard
Keyword(s):  
Acid Phosphatase ◽  
Stationary Phase ◽  
Leishmania Major ◽  
Enzymatic Characterization

Molecular and enzymatic characterization of acid phosphatase from venom of Scleroderma guani

2017 ◽  
Vol 20 (4) ◽  
pp. 1434-1441 ◽  
Author(s):  
Nai-Yong Liu ◽  
Xiao-Hong Fan ◽  
Zhi-Quan Zhang ◽  
Guo-Xing Wu ◽  
Jia-Ying Zhu
Keyword(s):  
Acid Phosphatase ◽  
Enzymatic Characterization

Structural and enzymatic characterization of plant zymogen bodies

1971 ◽  
Vol 49 (11) ◽  
pp. 2053-2057 ◽  
Author(s):  
Esther Cohen ◽  
Y. Shain ◽  
Y. Ben-Shaul ◽  
A. M. Mayer
Keyword(s):  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Galactosidase Activity ◽  
Enzymatic Characterization ◽  
Subcellular Organelles ◽  
Inactive Form ◽  
Optimum Ph ◽  
Membrane Bound ◽  
Pea Seeds

The zymogen body fraction of pea seeds was further investigated as to the content and localization of additional enzymes. This fraction was previously shown to contain an inactive form of amylopectin-1,6-glucosidase. An acid phosphatase was found with an optimum pH of 5.4. ATP or GTP were the preferred natural substrates, although there was no effect of Mg2+, K+, or Na+ ions on this acid nucleotide phosphatase activity. Cytochemical methods show that the ATPase is membrane-bound and that these bodies have only a single limiting membrane. No RNAse activity could be found; however, there was considerable β-galactosidase activity. It is concluded that these zymogen bodies are a distinct class of subcellular organelles in plants.

scholarly journals Identification and enzymatic characterization of acid phosphatase from Burkholderia gladioli

2014 ◽  
Vol 7 (1) ◽  
Author(s):  
Tiago Henrique Rombola ◽  
Eliamar Aparecida Nascimbem Pedrinho ◽  
Eliana Gertrudes de Macedo Lemos ◽  
Adriano Marques Gonçalves ◽  
Luiz Flávio José dos Santos ◽  
...  
Keyword(s):  
Acid Phosphatase ◽  
Enzymatic Characterization ◽  
Burkholderia Gladioli

Morphological Characterization of Mycobacteriophage R1

1974 ◽  
Vol 32 ◽  
pp. 254-255
Author(s):  
B. L. Soloff ◽  
T. A. Rado
Keyword(s):  
Carbon Source ◽  
Stationary Phase ◽  
Growth Phase ◽  
Minimal Medium ◽  
Morphological Characterization ◽  
Logarithmic Growth Phase ◽  
Complete Lysis ◽  
Lysogenic Culture ◽  
Logarithmic Growth

Mycobacteriophage R1 was originally isolated from a lysogenic culture of M. butyricum. The virus was propagated on a leucine-requiring derivative of M. smegmatis, 607 leu−, isolated by nitrosoguanidine mutagenesis of typestrain ATCC 607. Growth was accomplished in a minimal medium containing glycerol and glucose as carbon source and enriched by the addition of 80 μg/ ml L-leucine. Bacteria in early logarithmic growth phase were infected with virus at a multiplicity of 5, and incubated with aeration for 8 hours. The partially lysed suspension was diluted 1:10 in growth medium and incubated for a further 8 hours. This permitted stationary phase cells to re-enter logarithmic growth and resulted in complete lysis of the culture.

scholarly journals Enzymatic characterization of interferon-induced antiviral GTPases murine Mx1 and human MxA proteins.

1994 ◽  
Vol 269 (3) ◽  
pp. 2009-2015 ◽  
Author(s):  
K. Melén ◽  
T. Ronni ◽  
T. Lotta ◽  
I. Julkunen
Keyword(s):  
Enzymatic Characterization

scholarly journals Enzymatic Characterization of the N-Acetylation of 3-Phosphoglyceraldehyde Dehydrogenase by Acetyl Phosphate

1970 ◽  
Vol 245 (11) ◽  
pp. 2946-2953
Author(s):  
Jane Harting Park ◽  
Denis C. Shaw ◽  
Elizabeth Mathew ◽  
Blanche P. Meriwether
Keyword(s):  
Acetyl Phosphate ◽  
Enzymatic Characterization
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