scholarly journals Effect of X-irradiation on the Permeability of L-Alpha Hydroxy Acid Oxidase From Mouse Liver Peroxisomes

1974 ◽  
Vol 15 (4) ◽  
pp. 204-211
Author(s):  
P. C. BROWN ◽  
S. KLEINBERGS-KRISANS
Keyword(s):  
Hydroxy Acid ◽  
Mouse Liver ◽  
Acid Oxidase ◽  
X Irradiation ◽  
Liver Peroxisomes

The Effects of Whole-Body X-Irradiation on Mouse Liver Alpha-Hydroxy Acid Oxidase

1969 ◽  
Vol 40 (1) ◽  
pp. 213
Author(s):  
S. Kleinbergs ◽  
I. A. Bernstein
Keyword(s):  
Hydroxy Acid ◽  
Mouse Liver ◽  
Whole Body ◽  
Acid Oxidase ◽  
X Irradiation

scholarly journals THE SYNTHESIS AND TURNOVER OF RAT LIVER PEROXISOMES

1969 ◽  
Vol 41 (2) ◽  
pp. 521-535 ◽  
Author(s):  
Federico Leighton ◽  
Brian Poole ◽  
Paul B. Lazarow ◽  
Christian De Duve
Keyword(s):  
Amino Acid ◽  
Rat Liver ◽  
Isocitrate Dehydrogenase ◽  
Hydroxy Acid ◽  
Deae Cellulose ◽  
Urate Oxidase ◽  
Acid Oxidase ◽  
Total Proteins ◽  
Amino Acid Oxidase ◽  
Liver Peroxisomes

Rat liver peroxisomes isolated by density gradient centrifugation were disrupted at pH 9, and subdivided into a soluble fraction containing 90% of their total proteins and virtually all of their catalase, D-amino acid oxidase, L-α-hydroxy acid oxidase and isocitrate dehydrogenase activities, and a core fraction containing urate oxidase and 10% of the total proteins. The soluble proteins were chromatographed on Sephadex G-200, diethylaminoethyl (DEAE)-cellulose, hydroxylapatite, and sulfoethyl (SE)-Sephadex. None of these methods provided complete separation of the protein components, but these could be distributed into peaks in which the specific activities of different enzymes were substantially increased. Catalase, D-amino acid oxidase, and L-α-hydroxy acid oxidase contribute a maximum of 16, 2, and 4%, respectively, of the protein of the peroxisome. The contribution of isocitrate dehydrogenase could be as much as 25%, but is probably much less. After dissolution of the cores at pH 11 , no separation between their urate oxidase activity and their protein was achieved by Sephadex G-200 chromatography.

scholarly journals Basic Study on Active Changes in Biological Function of Mouse Liver Graft in Cold Storage after Low-Dose X-Irradiation

2009 ◽  
Vol 45 (2) ◽  
pp. 219-226 ◽  
Author(s):  
Takahiro Kataoka ◽  
Masaaki Yoshimoto ◽  
Shinya Nakagawa ◽  
Yuko Mizuguchi ◽  
Takehito Taguchi ◽  
...  
Keyword(s):  
Cold Storage ◽  
Mouse Liver ◽  
Low Dose ◽  
Biological Function ◽  
Liver Graft ◽  
Basic Study ◽  
X Irradiation

scholarly journals The localization of α-hydroxy acid oxidase in renal microbodies

1965 ◽  
Vol 160 (3) ◽  
pp. 329-344 ◽  
Author(s):  
John M. Allen ◽  
Margaret E. Beard ◽  
Skaidrite Kleinbergs
Keyword(s):  
Hydroxy Acid ◽  
Acid Oxidase

MD and QM/MM Studies on Long-Chain l-α-Hydroxy Acid Oxidase: Substrate Binding Features and Oxidation Mechanism

2014 ◽  
Vol 118 (20) ◽  
pp. 5406-5417 ◽  
Author(s):  
Yang Cao ◽  
Shuang Han ◽  
Lushan Yu ◽  
Haiyan Qian ◽  
Jian-Zhong Chen
Keyword(s):  
Hydroxy Acid ◽  
Substrate Binding ◽  
Oxidation Mechanism ◽  
Acid Oxidase ◽  
Long Chain

Studies on the L-2-hydroxy-acid oxidase 2 catalyzed metabolism of S-mandelic acid and its analogues

2019 ◽  
Vol 34 (3) ◽  
pp. 187-193
Author(s):  
Yang Zhang ◽  
Chen Su ◽  
Jinxiu Lei ◽  
Lu Chen ◽  
Haihong Hu ◽  
...  
Keyword(s):  
Hydroxy Acid ◽  
Mandelic Acid ◽  
Acid Oxidase
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