PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
7287656-8	1981	Hexadecane hydroxylation activity was solubilized from the intestinal microsomes and reconstituted with a partially purified cytochrome P-450 fraction, and intestinal NADPH-cytochrome c reductase, or spinach ferredoxin and ferredoxin-NADP reductase.	n-hexadecane	0-10	cytochrome P-450	Oryctolagus cuniculus	125-141	
7287656-9	1981	The chromatography of the crude cytochrome P-450 preparation on hydroxylapatite separated at least two cytochrome P-450 fractions; one preferentially hydroxylating hexadecane, and the other preferentially hydroxylating myristic acid.	n-hexadecane	164-174	cytochrome P-450	Oryctolagus cuniculus	32-48	
7287656-9	1981	The chromatography of the crude cytochrome P-450 preparation on hydroxylapatite separated at least two cytochrome P-450 fractions; one preferentially hydroxylating hexadecane, and the other preferentially hydroxylating myristic acid.	n-hexadecane	164-174	cytochrome P-450	Oryctolagus cuniculus	103-119	
7287656-10	1981	The results suggest that rabbit intestinal mucosa microsomes had a cytochrome P-450 species specialized for hexadecane hydroxylation.	n-hexadecane	108-118	cytochrome P-450	Oryctolagus cuniculus	67-83	
6766934-4	1980	Although another cytochrome P-450 fraction was active for hexadecane hydroxylation, this fraction had little activity.	n-hexadecane	58-68	cytochrome P-450	Oryctolagus cuniculus	17-33