Characterization of microsomal long-chain acyl-CoA hydrolase activity in the rat submandibular gland.
1. Long-chain fatty acyl-CoA hydrolase in submandibular gland microsomes was characterized and compared to that in liver ones. 2. In rat submandibular gland, the microsomal long-chain acyl-CoA hydrolase showed a higher relative activity for polyunsaturated fatty acyl-CoAs than that of liver microsomes. 3. It was suggested that the hydrolase in rat submandibular gland microsomes may play a role in modulation in the acyl-CoA pool size.
Shin
S O
SO
Department of Oral Biochemistry, Asahi University School of Dentistry, Gifu, Japan.
Kameyama
Y
Y
Yoshida
M
M
Takatsu
F
F
Shinkai
A
A
Inokuchi
H
H
Saito
Y
Y
Yokota
Y
Y
D000818:Animals; D008297:Male; D008563:Membrane Lipids / Q000737:chemistry; D008861:Microsomes / Q000201:enzymology*; D008862:Microsomes, Liver / Q000201:enzymology; D009928:Organ Specificity / Q000502:physiology; D010170:Palmitoyl-CoA Hydrolase / Q000032:analysis*; D010743:Phospholipids / Q000737:chemistry; D051381:Rats; D017208:Rats, Wistar; D013363:Submandibular Gland / Q000201:enzymology* / Q000648:ultrastructure; D013379:Substrate Specificity
D008563:Membrane Lipids; D010743:Phospholipids; D010170:Palmitoyl-CoA Hydrolase