Title : Characteristics of prolidase from the erythrocytes of normal humans and patients with prolidase deficiency and their mother.

Pub. Date : 2003 Oct

PMID : 14580160






7 Functional Relationships(s)
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Compound Name
Protein Name
Organism
1 Normal prolidase II was very labile in the absence of MnCl2 or mercaptoethanol. manganese chloride peptidase D Homo sapiens
2 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 peptidase D Homo sapiens
3 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 peptidase D Homo sapiens
4 The activity of prolidase I against glycylproline was enhanced strongly by glycine and MnCl2, but not activated in the absence of MnCl2. manganese chloride peptidase D Homo sapiens
5 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 peptidase D Homo sapiens
6 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 peptidase D Homo sapiens
7 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 peptidase D Homo sapiens