Isolation and characterization of some hydroxy fatty and phosphoric acid esters of 10-hydroxy-2-decenoic acid from the royal jelly of honeybees (Apis mellifera)

Lipids ◽  
2005 ◽  
Vol 40 (8) ◽  
pp. 833-838 ◽  
Author(s):  
Naoki Noda ◽  
Kazue Umebayashi ◽  
Takafumi Nakatani ◽  
Kazumoto Miyahara ◽  
Kaori Ishiyama
Apidologie ◽  
2012 ◽  
Vol 43 (6) ◽  
pp. 685-697 ◽  
Author(s):  
Takuma Matsuoka ◽  
Takuji Kawashima ◽  
Tadashi Nakamura ◽  
Yoshihiro Kanamaru ◽  
Tomio Yabe

Apidologie ◽  
2013 ◽  
Vol 45 (1) ◽  
pp. 143-143 ◽  
Author(s):  
Takuma Matsuoka ◽  
Takuji Kawashima ◽  
Tadashi Nakamura ◽  
Yoshihiro Kanamaru ◽  
Tomio Yabe

2013 ◽  
Vol 77 (4) ◽  
pp. 789-795 ◽  
Author(s):  
Tatsuya MORIYAMA ◽  
Miyako YANAGIHARA ◽  
Erika YANO ◽  
Goro KIMURA ◽  
Mariko SEISHIMA ◽  
...  

1990 ◽  
Vol 187 (2) ◽  
pp. 381-386 ◽  
Author(s):  
Peter CASTEELS ◽  
Christophe AMPE ◽  
Lise RIVIERE ◽  
Jose DAMME ◽  
Christopher ELICONE ◽  
...  

1980 ◽  
Vol 35 (9-10) ◽  
pp. 696-698 ◽  
Author(s):  
B. Schöbel ◽  
W. Pollmann

Abstract The characteristic features of an acetic acid esters hydrolyzing enzyme (acetylesterase, EC 3.1.1.16) are described. The pH- and temperature optimum were 7.0 and 40 °C respectively. The stability of the enzyme regarding different pH- and temperature conditions was investigated. The molecular weight of the acetylesterase could be determined to 160000. A small acetic ester hydrolyzing activity was found too with a molecular weight of about 25000. The activity was not inhibited by addition of di-isopropylphosphorofluoridate (DFP) or physostigmine. The KM-value for glyceryl triacetate was about 90 mM. Concentration of the enzyme was done by ultrafiltration and column-chromatography. The enzymatic activity tests were performed titrimetrically using glyceryl triacetate for substrate.


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