PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
4799079-2	1973	Drugs such as phenobarbitone and phenylbutazone, which increase the concentration of microsomal haem and cytochrome P-450, also increase the saturation of rat liver apo-(tryptophan pyrrolase) with its haem activator, as does the haem precursor 5-aminolaevulinate.	Phenobarbital	14-28	tryptophan 2,3-dioxygenase	Rattus norvegicus	170-190	
1751755-4	1991	Both phenobarbital and tryptophan increased tryptophan 2,3-dioxygenase activity (total enzyme and holoenzyme) but had different effects on the rate of activation and the degree of saturation of the enzyme with haem.	Phenobarbital	5-18	tryptophan 2,3-dioxygenase	Rattus norvegicus	44-70	
1751755-7	1991	It is proposed that combined administration of phenobarbital and tryptophan leads to substrate stabilisation of tryptophan 2,3-dioxygenase, and that this is accompanied by the binding of the newly synthesised haem, thus making haem unavailable for formation of cytochrome P-450.	Phenobarbital	47-60	tryptophan 2,3-dioxygenase	Rattus norvegicus	112-138	
4768733-0	1973	Tryptophan pyrrolase in rat liver after phenobarbital administration.	Phenobarbital	40-53	tryptophan 2,3-dioxygenase	Rattus norvegicus	0-20	
7197926-2	1981	Chronic administration of morphine, nicotine or phenobarbitone has previously been shown to inhibit rat liver tryptophan pyrrolase activity by increasing hepatic [NADPH], whereas subsequent withdrawal enhances pyrrolase activity by a hormonal-type mechanism.	Phenobarbital	48-62	tryptophan 2,3-dioxygenase	Rattus norvegicus	110-130