3.4.23.1	additional information	-	-	35005, 36736, 36742, 36754	
3.4.23.1	0.5	3.5	N,N-dimethylhemoglobin, pH 0.5: about 30% of maximum activity, pH 3.5: about 15% of maximum activity	36758	
3.4.23.1	0.5	5	N,N-dimethylcasein, pH 0.5: about 35% of maximum activity, pH 5.0: about 20% of maximum activity	36758	
3.4.23.1	1	3.5	-	36748	
3.4.23.1	1	3.5	pH 1.0: about 85% of maximal activity, pH 3.5: about 40% of maximal activity	679796	
3.4.23.1	1	4	pH 1.0: about 70% of maximal activity, pH 4.0: about 50% of maximal activity	679796	
3.4.23.1	1	6	trout pepsins exhibit the highest enzyme activity at pH 3.0 (isoform P-I) and 2.5 (isoforms P-II and P-III); P-I shows a broad optimum in the pH range from 1.5 to 4.0, while the optima for P-II and III are restricted to the pH range from 2.0 to 3.0.at pH 4.0. Isoform P-I retains 94% activity, while isoforms P-II 72 and P-III have 65% activity. All three isoforms show residual activity of about 20% at pH 6.0	753464	
3.4.23.1	1.5	3.5	highly active between pH 1.5-3.5	753325	
3.4.23.1	1.5	4	pH 1.5: about 75% of maximum activity, pH 4.0: about 30% of maximum activity	36755	
3.4.23.1	1.5	4.5	pH 1.5: about 90% of maximum activity, pH 4.5: about 35% of maximum activity	36739	
3.4.23.1	1.6	2.2	-	36768	
3.4.23.1	2	5	with serum albumin as a substrate, the enzyme retains 70% of its activity at pH 4.0 and almost 40% at pH 5.0	753393	
3.4.23.1	2.1	4.5	pH optimum for selective digestion of collagen telopeptides	754305	
3.4.23.1	2.5	4	pH 2.5: about 55% of maximal activity, pH 4.0: about 55% of maximal activity	679335	
3.4.23.1	3	5	maximum activity towards this substrate at pH values between pH 3.5 and 4.0, with a drastic decrease in activity of 50% and 70% at pH values 3.0 and 5.0, respectively	755425	
3.4.23.1	3.5	5	50% activity is retained at pH 5.0 At pH 6.0, the enzyme shows no activity	717595