3.4.22.14	1-(L-trans-epoxysuccinylleucylamino)-4-guanidinobutane	-	12946	
3.4.22.14	1-(L-trans-epoxysuccinylleucylamino)-4-guanidinobutane	potent, highly selective, irreversible	12946	
3.4.22.14	4,4'-dithiodipyridine	-	6845	
3.4.22.14	5,5'-dithiobis(2-nitrobenzoic acid)	-	221	
3.4.22.14	Ba2+	addition leads to inhibition of free actinidin whereas immobilized actinidin shows a much weaker inhibition	111	
3.4.22.14	Ca2+	addition leads to inhibition of free actinidin whereas immobilized actinidin shows a much weaker inhibition	15	
3.4.22.14	Cd2+	-	52	
3.4.22.14	Co2+	addition leads to inhibition of free actinidin whereas immobilized actinidin shows a much weaker inhibition	23	
3.4.22.14	Cu2+	-	19	
3.4.22.14	cystatin	hybrids of chicken cystatin with human kininogen domain 2 sequences exhibit improved inhibition	1600	
3.4.22.14	cystatin C	recombinant inhibitor expressed in E. coli	1994	
3.4.22.14	E-64	-	559	
3.4.22.14	Fe2+	addition leads to inhibition of free actinidin whereas immobilized actinidin shows a much weaker inhibition	25	
3.4.22.14	Hg2+	-	33	
3.4.22.14	human kininogen domain 2	hybrids of chicken cystatin with human kininogen domain 2 sequences exhibit improved inhibition	100713	
3.4.22.14	iodoacetate	-	93	
3.4.22.14	KCl	minimal activity at 0.5-0.8 M, depending on substrate concentration. Minimal activity is 50-70% of the acitivity in absence of salt, with increase in KM-value and decrease in kcat-value. Slight reactivation above 0.8 M	79	
3.4.22.14	L-kininogen	-	11007	
3.4.22.14	leupeptin	-	217	
3.4.22.14	LiCl	minimal activity at 1.0-1.5 M, depending on substrate concentration. Minimal activity is 50-70% of the acitivity in absence of salt, with increase in KM-value and decrease in kcat-value. Slight reactivation above 1.5 M	815	
3.4.22.14	Mg2+	addition leads to inhibition of free actinidin whereas immobilized actinidin shows a much weaker inhibition	6	
3.4.22.14	Mn2+	addition leads to inhibition of free actinidin whereas immobilized actinidin shows a much weaker inhibition	11	
3.4.22.14	N-(trans-epoxysuccinyl)-L-leucine 4-guanidinobutylamide	conformational mobility of actinidin changes upon binding of the inhibitor E-64, leading to a sequence of events that enables water and ions to protrude into a newly formed cavity of the inhibited enzyme	206268	
3.4.22.14	N-(trans-epoxysuccinyl)-L-leucine 4-guanidinobutylamide	in contrast to actinidin without inhibitor, the actinidin–E-64 complex starts degrading 15 min after incubation in simulated gastric fluid (SGF) and is fully degraded after 60 min of incubation. In addition transition maximum temperature (Tm) of the actinidin-inhibitor complex is 61°C in contrast to Tm: 73.9° of actinidin without inhibitor	206268	
3.4.22.14	N-acetyl-L-Arg	-	20394	
3.4.22.14	N-benzoyl-L-Arg	-	15861	
3.4.22.14	N-benzoyl-L-Arg ethyl ester	-	10722	
3.4.22.14	NaCl	minimal activity at 0.5-1.2 M, depending on substrate concentration. Minimal activity is 50-70% of the acitivity in absence of salt, with increase in KM-value and decrease in kcat-value. Slight reactivation above 1.2 M	42	
3.4.22.14	PCMB	-	78	
3.4.22.14	Zn2+	addition leads to inhibition of free actinidin whereas immobilized actinidin shows a much weaker inhibition	14	
3.4.22.14	Zn2+	-	14