scholarly journals Purification and Characterization of Aspartate Aminotransferase Isoenzymes from Rice Bran

1993 ◽  
Vol 57 (12) ◽  
pp. 2074-2080 ◽  
Author(s):  
Toshiharu Yagi ◽  
Masayuki Sako ◽  
Shinya Moriuti ◽  
Masafumi Shounaka ◽  
Kazunari Masaki ◽  
...  
Keyword(s):  
Rice Bran ◽  
Aspartate Aminotransferase ◽  
Purification And Characterization

Simultaneous Purification and Characterization of Aspartate Aminotransferase Isoenzymes from Chicken Liver

Enzyme ◽  
1988 ◽  
Vol 40 (4) ◽  
pp. 189-197 ◽  
Author(s):  
R. Gracia ◽  
M. Busquets ◽  
M. Gil ◽  
A. Cortés ◽  
J. Bozal
Keyword(s):  
Aspartate Aminotransferase ◽  
Chicken Liver ◽  
Purification And Characterization

scholarly journals Purification and characterization of aspartate aminotransferase from the halophile archaebacterium Haloferax mediterranei

1991 ◽  
Vol 278 (1) ◽  
pp. 149-154 ◽  
Author(s):  
F J G Muriana ◽  
M C Alvarez-Ossorio ◽  
A M Relimpio
Keyword(s):  
Aspartate Aminotransferase ◽  
Maximum Activity ◽  
Purification And Characterization ◽  
Scanning Calorimetry ◽  
Haloferax Mediterranei ◽  
First Order Kinetics ◽  
Low Salt ◽  
Titration Data ◽  
Ph Range

Aspartate aminotransferase from the archaebacterium Haloferax mediterranei was purified and found to be homogeneous. An average Mr of 66,000 was estimated. The native halophilic transaminase exhibited no maximum absorption at 410 nm, which indicates that the apo form is obtained by our purification procedure, and the molar absorption coefficient at 275 nm in 3.5 M-KCl (pH 7.8) was found to be 78.34 mM-1.cm-1. Plots of titration data show that 1 mol of halophilic aspartate aminotransferase binds 2 mol of pyridoxal 5′-phosphate. The halophilic transaminase behaved as a dimer with two similar subunits and had a maximum activity in the pH range 7.6-7.9 and at 65 degrees C in 3.5 M-KCl. By differential scanning calorimetry, the denaturation temperature of the halophilic holo- and apo-transaminase was determined to be 78.5 and 68.0 degrees C respectively at 3.3 M-KCl (pH 7.8). At low salt concentration the halophilic transaminase was inactivated, following first-order kinetics. The Km values for 2-oxoglutarate and L-aspartate, in 3 M-KCl (pH 7.8), were 0.75 mM and 12.6 mM respectively.

scholarly journals Biochemical studies on rice bran lipase. IV. Purification and characterization of rice bran lipase II.

1976 ◽  
Vol 40 (2) ◽  
pp. 317-324 ◽  
Author(s):  
Yasuo AIZONO ◽  
Masaru FUNATSU ◽  
Yukio FUJIKI ◽  
Masayoshi WATANABE
Keyword(s):  
Rice Bran ◽  
Purification And Characterization ◽  
Biochemical Studies ◽  
Rice Bran Lipase

Purification and characterization of antioxidative peptides derived from rice bran protein hydrolysates

2008 ◽  
Vol 228 (4) ◽  
pp. 553-563 ◽  
Author(s):  
Abayomi Peter Adebiyi ◽  
Ayobamitale O. Adebiyi ◽  
Junko Yamashita ◽  
Tomohisa Ogawa ◽  
Koji Muramoto
Keyword(s):  
Rice Bran ◽  
Protein Hydrolysates ◽  
Purification And Characterization ◽  
Rice Bran Protein

scholarly journals Purification and Characterization, of Rice Bran Lipase II

1976 ◽  
Vol 40 (2) ◽  
pp. 317-324 ◽  
Author(s):  
Yasuo Aizono ◽  
Masaru Funatsu ◽  
Yukio Fujiki ◽  
Masayoshi Watanabe
Keyword(s):  
Rice Bran ◽  
Purification And Characterization ◽  
Rice Bran Lipase
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