Purification and characterization of α2-macroglobulin from the white shrimp (Penaeus vannamei)

2003 ◽  
Vol 134 (4) ◽  
pp. 431-438 ◽  
Author(s):  
Teresa Gollas-Galván ◽  
Rogerio R. Sotelo-Mundo ◽  
Gloria Yepiz-Plascencia ◽  
Claudia Vargas-Requena ◽  
Francisco Vargas-Albores
Keyword(s):  
White Shrimp ◽  
Penaeus Vannamei ◽  
Purification And Characterization ◽  
Α2 Macroglobulin

Purification and characterization of the clotting protein from the white shrimp Penaeus vannamei

1999 ◽  
Vol 122 (4) ◽  
pp. 381-387 ◽  
Author(s):  
Karla Montaño-Pérez ◽  
Gloria Yepiz-Plascencia ◽  
Inocencio Higuera-Ciapara ◽  
Francisco Vargas-Albores
Keyword(s):  
White Shrimp ◽  
Penaeus Vannamei ◽  
Purification And Characterization ◽  
Clotting Protein

Characterization of a novel shrimp pathogen, Vibrio brasiliensis , isolated from Pacific white shrimp, Penaeus vannamei

2021 ◽  
Author(s):  
Ge Li ◽  
Guosi Xie ◽  
Hailiang Wang ◽  
Xiaoyuan Wan ◽  
Xinshu Li ◽  
...  
Keyword(s):  
Pacific White Shrimp ◽  
White Shrimp ◽  
Penaeus Vannamei

Purification and Characterization of Trypsin from Hepatopancreas of Pacific White Shrimp

2015 ◽  
Vol 39 (4) ◽  
pp. 388-397 ◽  
Author(s):  
Theeraphol Senphan ◽  
Soottawat Benjakul ◽  
Hideki Kishimura
Keyword(s):  
Pacific White Shrimp ◽  
White Shrimp ◽  
Purification And Characterization

Molecular characterization of the bifunctional VHDL-CP from the hemolymph of white shrimp Penaeus vannamei

2002 ◽  
Vol 132 (3) ◽  
pp. 585-592 ◽  
Author(s):  
Gloria Yepiz-Plascencia ◽  
Florinda Jiménez-Vega ◽  
Marı́a Gabriela Romo-Figueroa ◽  
Rogerio R Sotelo-Mundo ◽  
Francisco Vargas-Albores
Keyword(s):  
Molecular Characterization ◽  
White Shrimp ◽  
Penaeus Vannamei

Purification and characterization of a lectin from the white shrimp Litopenaeus setiferus (Crustacea decapoda) hemolymph

2005 ◽  
Vol 1724 (1-2) ◽  
pp. 86-93 ◽  
Author(s):  
Juan Alpuche ◽  
Ali Pereyra ◽  
Concepción Agundis ◽  
Carlos Rosas ◽  
Cristina Pascual ◽  
...  
Keyword(s):  
White Shrimp ◽  
Purification And Characterization ◽  
Litopenaeus Setiferus

Purification and Characterization of Kallikrein from Plasma of Patients with Acute Pancreatitis

1981 ◽  
Vol 60 (2) ◽  
pp. 199-205 ◽  
Author(s):  
Naotika Toki ◽  
Hiroyuki Sumi ◽  
Sumiyoshi Takasugi
Keyword(s):  
Acute Pancreatitis ◽  
Specific Activity ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Gel Filtration ◽  
Apparent Molecular Weight ◽  
Purification And Characterization ◽  
Α2 Macroglobulin ◽  
Sepharose 4B

1. A kallikrein-like enzyme in plasma of patients with acute pancreatitis was further purified by successive hydroxyapatite/cellulose and Sepharose-4B column chromatography. 2. By these procedures 0.26 mg of purified enzyme with a specific activity of 215 S-2266 chromozyme units/mg of protein was obtained from 10 ml of original plasma. 3. The purified material was homogeneous as ascertained by sodium dodecyl sulphate/polyacrylamide-gel electrophoresis and had an apparent molecular weight of 31 000 as measured by gel filtration on Sephadex G-200. 4. It was confirmed immunologically that this enzyme was pancreatic kallikrein, which is distinct from plasma kallikrein, and that it could combine with α2-macroglobulin only in the presence of trypsin.

scholarly journals Purification and characterization of an α2-macroglobulin-like proteinase inhibitor from plasma of the crayfish Pacifastacus leniusculus

1988 ◽  
Vol 255 (3) ◽  
pp. 801-806 ◽  
Author(s):  
H G Hergenhahn ◽  
M Hall ◽  
K Söderhäll
Keyword(s):  
Proteinase Inhibitor ◽  
Hydrophobic Interaction Chromatography ◽  
Acid Precipitation ◽  
Anion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Pacifastacus Leniusculus ◽  
Purification And Characterization ◽  
Apparent Homogeneity ◽  
Α2 Macroglobulin

An alpha 2-macroglobulin (alpha 2M)-like proteinase inhibitor from plasma of the crayfish Pacifastacus leniusculus was purified to apparent homogeneity by acid precipitation, hydrophobic interaction chromatography, affinity chromatography on concanavalin A-Sepharose and anion-exchange chromatography. The subunit Mr is about 190,000. Pore-size-limit electrophoresis proved the native protein to be a dimer. The purified protein resembled vertebrate alpha 2 Ms in that it protected trypsin from inhibition by soyabean trypsin inhibitor, and in its sensitivity to methylamine treatment. Methylamine also prevented the protein from being autolytically cleaved into Mr 60,000 and 140,000 fragments when subjected to heat treatment. The amino acid composition showed similarities with both human alpha 2 M and an alpha 2 M-like protein from the arthropod Limulus polyphemus. These data indicate that this Pacifastacus alpha 2M-like protein (P alpha 2M) may be a distantly related homologue of vertebrate alpha 2Ms.

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