PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
15530480-3	2004	Effects of various amino acids and their metabolites on prolidase activity against iminodipeptides in presence of 1 mmol/l MnCl(2) were investigated.	manganese chloride	123-130	peptidase D	Homo sapiens	56-65	
1551457-6	1992	The activity of prolidase I, eluted at the lowest ionic strength, was stimulated by 24 hr of preincubation with 1 mM MnCl2, but prolidase II activity was strongly inhibited by this long preincubation.	manganese chloride	117-122	peptidase D	Homo sapiens	16-25	
3205627-8	1988	After exogenous MnCl2 is removed from the storage buffer, high levels of erythrocyte prolidase activity persist for at least 13 days.	manganese chloride	16-21	peptidase D	Homo sapiens	85-94	
14580160-3	2003	Normal prolidase II was very labile in the absence of MnCl2 or mercaptoethanol.	manganese chloride	54-59	peptidase D	Homo sapiens	7-16	
15552267-4	2004	The same studies on erythrocytes from a prolidase-deficient patient showed almost the same results as the normal control, except that prolinase activity against pro-gly and pro-ser was slightly inhibited by adding 0.1 mM MnCl2.	manganese chloride	221-226	peptidase D	Homo sapiens	40-49	
14580160-4	2003	The activity of prolidase II was maintained at about 76% by pre-incubation with MnCl2; it was then activated up to 140% by treatment with mercaptoethanol for 60 minutes at 37 degrees C. Normal prolidases I and II showed the highest activity against glycylproline or methionylproline in the presence of MnCl2.	manganese chloride	80-85	peptidase D	Homo sapiens	16-25	
14580160-4	2003	The activity of prolidase II was maintained at about 76% by pre-incubation with MnCl2; it was then activated up to 140% by treatment with mercaptoethanol for 60 minutes at 37 degrees C. Normal prolidases I and II showed the highest activity against glycylproline or methionylproline in the presence of MnCl2.	manganese chloride	302-307	peptidase D	Homo sapiens	16-25	
14580160-5	2003	The activity of prolidase I against glycylproline was enhanced strongly by glycine and MnCl2, but not activated in the absence of MnCl2.	manganese chloride	87-92	peptidase D	Homo sapiens	16-25	
14580160-6	2003	The activity of prolidase II against methionylproline was enhanced three-fold in the presence of glycine and MnCl2, but its activity against glycylproline was very low even in the presence of MnCl2.	manganese chloride	109-114	peptidase D	Homo sapiens	16-25	
14580160-6	2003	The activity of prolidase II against methionylproline was enhanced three-fold in the presence of glycine and MnCl2, but its activity against glycylproline was very low even in the presence of MnCl2.	manganese chloride	192-197	peptidase D	Homo sapiens	16-25	
14580160-8	2003	The activity of prolidase II against methionylproline in all erythrocytes, of normal humans and of patients, was strongly activated by the addition of glycine with MnCl2 but suppressed by the addition of mercaptoethanol.	manganese chloride	164-169	peptidase D	Homo sapiens	16-25	
12433302-5	2002	The results obtained showed that the prolidase-loaded PLGA microspheres can be prepared only upon enzyme stabilization by addition of both BSA and MnCl(2) into its TRIS solution.	manganese chloride	147-154	peptidase D	Homo sapiens	37-46