scholarly journals Purification and characterization of Clostridium perfringens iota toxin: dependence on two nonlinked proteins for biological activity.

1986 ◽  
Vol 54 (3) ◽  
pp. 683-688 ◽  
Author(s):  
B G Stiles ◽  
T D Wilkins
Keyword(s):  
Biological Activity ◽  
Clostridium Perfringens ◽  
Purification And Characterization ◽  
Clostridium Perfringens Iota Toxin

Purification and characterization of a recombinant α-N-acetylgalactosaminidase from Clostridium perfringens

2003 ◽  
Vol 32 (2) ◽  
pp. 309-316 ◽  
Author(s):  
Hsin-Yeh Hsieh ◽  
Michael J Calcutt ◽  
Linda F Chapman ◽  
Moonmoon Mitra ◽  
Daniel S Smith
Keyword(s):  
Clostridium Perfringens ◽  
Purification And Characterization

Purification and Characterization of α-N-Acetylgalactosaminidase from Clostridium perfringens

IUBMB Life ◽  
2000 ◽  
Vol 50 (2) ◽  
pp. 91-97
Author(s):  
Hsin-Yeh Hsieh ◽  
Moonmoon Mitra ◽  
Donald Charles Wells ◽  
Daniel Smith
Keyword(s):  
Clostridium Perfringens ◽  
Purification And Characterization

scholarly journals Purification and characterization of guinea-pig intestinal brush borders

1975 ◽  
Vol 152 (1) ◽  
pp. 157-159 ◽  
Author(s):  
K Andersen ◽  
G V Lippe ◽  
L Morkrid ◽  
H Schjonsby
Keyword(s):  
Biological Activity ◽  
Guinea Pig ◽  
Gradient Centrifugation ◽  
Fold Increase ◽  
Prolonged Storage ◽  
Purification And Characterization ◽  
Brush Borders ◽  
Centrifugation Step ◽  
Vitamin B 12

The purification of guinea-pig intestinal brush borders by a rapid sucrose-gradient-centrifugation step is reported. A 29-fold increase in the maltase/DNA quotient indicates considerable purification of the brush borders from nuclei. The biological activity of the brush borders was well preserved, as demonstrated by a high recovery of human gastric-juice-mediated uptake of 57Co-labelled vitamin B-12; homogeneity and purity were confirmed by scanning electron microscopy. Both the morphological appearance and biological activity were unchanged after prolonged storage in glycerol.

scholarly journals Purification and Characterization of a Monooxygenase Involved in the Biosynthetic Pathway of the Antitumor Drug Mithramycin

2003 ◽  
Vol 185 (13) ◽  
pp. 3962-3965 ◽  
Author(s):  
David Rodríguez ◽  
Luis M. Quirós ◽  
Alfredo F. Braña ◽  
José A. Salas
Keyword(s):  
Biological Activity ◽  
Biosynthetic Pathway ◽  
Flavin Adenine Dinucleotide ◽  
Chain Molecule ◽  
Aliphatic Chain ◽  
Purification Procedure ◽  
Reaction Products ◽  
Purification And Characterization ◽  
Optimal Ph

ABSTRACT A monooxygenase encoded by the mtmOIV gene from the mithramycin gene cluster of Streptomyces argillaceus was purified 21-fold by a three-step purification procedure. This monooxygenase catalyzes the oxidative cleavage of the fourth ring of premithramycin B. The enzyme was dependent on NADPH and flavin adenine dinucleotide for activity with optimal pH at 9.5, and the Km values for NADPH and premithramycin B were 269.22 and 23.35 μM, respectively. The reaction catalyzed by MtmOIV yields two possible isomers of the same basic shortened aliphatic chain molecule. One of the reaction products showed important biological activity, thus highlighting the importance of the cleavage of the fourth ring of the aglycon for biological activity.

Purification and characterization of fucose-containing sulphated polysaccharides from Sargassum tenerrimum and their biological activity

2019 ◽  
Vol 31 (5) ◽  
pp. 3101-3113
Author(s):  
Manoj Saravana Guru Mohan ◽  
Anant Achary ◽  
Vasanthi Mani ◽  
Eduardas Cicinskas ◽  
Aleksandra A. Kalitnik ◽  
...  
Keyword(s):  
Biological Activity ◽  
Purification And Characterization ◽  
Sulphated Polysaccharides ◽  
Sargassum Tenerrimum
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