scholarly journals Molecular and Biochemical Characterization of AtPAP15, a Purple Acid Phosphatase with Phytase Activity, in Arabidopsis

2009 ◽  
Vol 151 (1) ◽  
pp. 199-209 ◽  
Author(s):  
Ruibin Kuang ◽  
Kam-Ho Chan ◽  
Edward Yeung ◽  
Boon Leong Lim
1977 ◽  
Vol 23 (1) ◽  
pp. 89-94 ◽  
Author(s):  
K W Lam ◽  
L T Yam

Abstract A tartrate-resistant acid phosphatase was isolated from a human leukemic spleen by freeze-thawing in saline and purified by repeated chromatography on carboxymethyl-cellulose. The purified enzyme has a molecular weight of 64 000. It catalyzes the hydrolysis of inorganic and organic pyrophosphate as well as the phenolic ester of monoorthophosphate, with optimal activity between pH 5 and 6. However, there is no activity toward mono-orthophosphate esters of aliphatic alcohols. The present data have identified its catalytic function as a pyrophosphatase. However, it has properties different from the pyrophosphatase previously observed in normal animal tissues.


2009 ◽  
Vol 152 (2) ◽  
pp. 854-865 ◽  
Author(s):  
Cuiyue Liang ◽  
Jiang Tian ◽  
Hon-Ming Lam ◽  
Boon Leong Lim ◽  
Xiaolong Yan ◽  
...  

2008 ◽  
Vol 69 (2) ◽  
pp. 365-373 ◽  
Author(s):  
Shiu-Cheung Lung ◽  
Andy Leung ◽  
Rainbow Kuang ◽  
Yu Wang ◽  
Priscilla Leung ◽  
...  

1964 ◽  
Vol s3-105 (69) ◽  
pp. 73-78
Author(s):  
J. V. DIENGDOH

Lysosomes, as demonstrated biochemically in the liver, are subcellular particles containing a group of hydrolytic enzymes enclosed by a membrane-like barrier. They are apparently inactive in the normal state, but when subjected to various forms of injurious treatments the enzymes associated with them are released. The existence of lysosomes in skin is demonstrated in the present communication. The resistance of this tissue to homogenization makes the biochemical study of lysosomes very difficult. Yet, by the application of histochemical methods to sections of skin, it has been possible to use the same criteria as would be employed in the biochemical characterization of these organelles. By using the controlled-temperature freezing-sectioning method it has been possible to obtain frozen sections in which cytoplasmic particles could be demonstrated which were enzymically inactive for acid phosphatase until the sections were subjected to such injurious treatments as heat, repeated freezing and thawing, hypotonic solutions, distilled water, and ‘triton-X-100’. Since the subcellular particles demonstrated behaved in the same manner as lysosomes prepared biochemically from liver, it is concluded that the cytoplasmic organelles staining for acid phosphatase in mouse skin are lysosomes as biochemically defined.


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