Relative enzymatic hydrolysis rates of lincomycin esters I: Soluble esters

✍ Scribed by Mildred J. Taraszka

• Publisher: John Wiley and Sons
• Year: 1971
• Tongue: English
• Weight: 389 KB
• Volume: 60
• Category: Article
• ISSN: 0022-3549
• DOI: 10.1002/jps.2600600929

✦ Synopsis

Enzymatic hydrolysis rates were determined for different positional and structural esters of lincomycin in dog serum and simulated intestinal fluid USP. In general, the hydrolysis rates were faster in simulated intestinal Auid than in dog serum, indicating a higher esterase activity in simulated intestinal fluid. The order of hydrolysis rates for positional lincomycin monohexanoate esters was 2 >> 3 > 4 , -7 in simulated intestinal fluid and 2 > 3 N 4 > 7 in dog serum. The 2-propionate ester of lincomycin was hydrolyzed slower than the longer chain 2-hexanoate ester, with the greatest difference in rates occurring in simulated intestinal fluid. Sterically hindered esters, e.g., lincomycin-2-pivalate and lincomycin-2-( 3,3dimethyl)butyrate, were hydrolyzed at extremely slow rates. The significance of the relative hydrolysis rates when compared to the in vivo activity of the esters is discussed.