Separation and partial purification of collagenolytic protease from peacock bass (Cichla ocellaris) using different protocol: Precipitation and partitioning approaches

2020 ◽  
Vol 24 ◽  
pp. 101509
Author(s):  
Vagne de Melo Oliveira ◽  
Márcia Nieves Carneiro da Cunha ◽  
Caio Rodrigo Dias de Assis ◽  
Juanize Matias da Silva Batista ◽  
Thiago Pajeú Nascimento ◽  
...  
Keyword(s):  
Partial Purification ◽  
Collagenolytic Protease ◽  
Peacock Bass ◽  
Cichla Ocellaris

Butterfly peacock bass, Cichla ocellaris (Bloch & Schneider 1801)

Peacock Bass ◽  
2021 ◽  
pp. 33-64
Author(s):  
Kirk O. Winemiller ◽  
Leslie C. Kelso Winemiller ◽  
Carmen G. Montaña
Keyword(s):  
Peacock Bass ◽  
Cichla Ocellaris

Evaluating effects of catch-and-release angling on peacock bass (Cichla ocellaris) in a Puerto Rican reservoir: A rapid assessment approach

2016 ◽  
Vol 175 ◽  
pp. 95-102 ◽  
Author(s):  
Shannon D. Bower ◽  
Andy J. Danylchuk ◽  
Jacob W. Brownscombe ◽  
Jason D. Thiem ◽  
Steven J. Cooke
Keyword(s):  
Puerto Rican ◽  
Rapid Assessment ◽  
Catch And Release ◽  
Assessment Approach ◽  
Peacock Bass ◽  
Cichla Ocellaris

Kinetic and physicochemical properties of brain acetylcholinesterase from the peacock bass (Cichla ocellaris) and in vitro effect of pesticides and metal ions

2013 ◽  
Vol 126 ◽  
pp. 191-197 ◽  
Author(s):  
Kaline Catiely Campos Silva ◽  
Caio Rodrigo Dias Assis ◽  
Vagne Melo Oliveira ◽  
Luiz Bezerra Carvalho ◽  
Ranilson Souza Bezerra
Keyword(s):  
Physicochemical Properties ◽  
Metal Ions ◽  
Vitro Effect ◽  
Peacock Bass ◽  
Brain Acetylcholinesterase ◽  
Cichla Ocellaris

scholarly journals Microbiota of two species of commercially important fish in the Amazon region (Belm-Par-Brazil): Butterfly peacock bass (Cichla ocellaris) and piramutaba (Brachyplatystoma vailantii)

2015 ◽  
Vol 9 (9) ◽  
pp. 572-580 ◽  
Author(s):  
Ivana Trindade Damasceno Evelyn ◽  
Natasha da Gama Pantoja Lauana ◽  
Mendes de Figueiredo Hamilton ◽  
Helena Meller da Silva Luiza ◽  
Manoel da Cruz Rodrigues Antonio
Keyword(s):  
Amazon Region ◽  
Commercially Important ◽  
Peacock Bass ◽  
Important Fish ◽  
Cichla Ocellaris

Heavy Metal Accumulation in the Intestinal Tapeworm Proteocephalus macrophallus Infecting the Butterfly Peacock Bass (Cichla ocellaris), from Southeastern Brazil

2019 ◽  
Vol 103 (5) ◽  
pp. 670-675
Author(s):  
Lucas A. R. Leite ◽  
Felipe F. Januário ◽  
Pedro M. Padilha ◽  
Emmyle T. C. do Livramento ◽  
Rodney K. de Azevedo ◽  
...  
Keyword(s):  
Heavy Metal ◽  
Metal Accumulation ◽  
Heavy Metal Accumulation ◽  
Southeastern Brazil ◽  
Peacock Bass ◽  
Cichla Ocellaris

Partial purification and properties of an endo-xylanase from cucumber seeds

1991 ◽  
Vol 81 (3) ◽  
pp. 327-334 ◽  
Author(s):  
Cesar V. Mujer ◽  
Dale W. Kretchman ◽  
A. Raymond Miller
Keyword(s):  
Partial Purification ◽  
Purification And Properties

Partial purification and properties of a 36-kDa 1-aminocyclopropane-l-carboxylate N-malonyltransferase from mung bean

1995 ◽  
Vol 94 (4) ◽  
pp. 629-634 ◽  
Author(s):  
Mohamed Benichou ◽  
Gracia Martinez-Reina ◽  
Felix Romojaro ◽  
Jean-Claude Pech ◽  
Alain Latche
Keyword(s):  
Mung Bean ◽  
Partial Purification ◽  
Purification And Properties

Studies on an Inhibitor of Plasminogen Activation in Human Serum

1973 ◽  
Vol 30 (02) ◽  
pp. 414-424 ◽  
Author(s):  
Ulla Hedner
Keyword(s):  
Ion Exchange ◽  
Human Serum ◽  
Antithrombin Iii ◽  
Gel Filtration ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Specific Adsorption ◽  
Partial Purification ◽  
Plasminogen Activation ◽  
Preparative Electrophoresis

SummaryA procedure is described for partial purification of an inhibitor of the activation of plasminogen by urokinase and streptokinase. The method involves specific adsorption of contammants, ion-exchange chromatography on DEAE-Sephadex, gel filtration on Sephadex G-200 and preparative electrophoresis. The inhibitor fraction contained no antiplasmin, no plasminogen, no α1-antitrypsin, no antithrombin-III and was shown not to be α2 M or inter-α-inhibitor. It contained traces of prothrombin and cerulo-plasmin. An antiserum against the inhibitor fraction capable of neutralising the inhibitor in serum was raised in rabbits.

Plasminogen-Activator in Human Early Milk: Its Partial Purification and Characterization

1981 ◽  
Vol 45 (02) ◽  
pp. 121-126 ◽  
Author(s):  
Utako Okamoto ◽  
Noboru Horie ◽  
Yoko Nagamatsu ◽  
Jun-Ichiro Yamamoto
Keyword(s):  
Plasminogen Activator ◽  
Polyacrylamide Gel Electrophoresis ◽  
Gel Filtration ◽  
Partial Purification ◽  
Order Kinetic ◽  
Diisopropyl Fluorophosphate ◽  
Step Procedure ◽  
Activity Band ◽  
C 50 ◽  
Gel Isoelectric Focusing

SummaryMilk plasminogen-activator was partially purified from human transitional milk collected at about 10 days after delivery, by a five-step procedure involving chloroform treatment, ammonium sulfate precipitation, and column chromatography on Sephadex G-150, CM Sephadex C-50 and DEAE Sephadex A-50. This gave milk-activator with a maximum purification factor of about 2,400-fold with respect to the skimmed milk. The CM Sephadex-step preparation showed, on polyacrylamide gel electrophoresis, a single plasminogen-activator activity band located between the bands of albumin and prealbumin of human serum. This preparation exhibited no kinin forming activity. The activator hydrolyzed acetyl-glycyl-L-lysine methyl ester with similar order kinetic constants to urokinase, and was inhibited strongly by diisopropyl-fluorophosphate. The molecular weight of the activator as estimated by gel filtration was approximately 86,000, the isoelectric points as estimated by gel isoelectric focusing were pH 7.2, 6.9 and 6.6, and the activator activity was not quenched by antiurokinase globulin, indicating that the milk-activator is a different entity from urokinase.

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