Purification and characterization of one of the forms of peptide hydrolases from guinea-pig small intestinal mucosa

1973 ◽  
Vol 327 (2) ◽  
pp. 425-436 ◽  
Author(s):  
J. Donlon ◽  
P.F. Fottrell
Keyword(s):  
Guinea Pig ◽  
Intestinal Mucosa ◽  
Small Intestinal Mucosa ◽  
Purification And Characterization ◽  
Small Intestinal ◽  
Peptide Hydrolases

scholarly journals Human small-intestinal β-galactosidases. Separation and characterization of one lactase and one hetero β-galactosidase

1969 ◽  
Vol 114 (2) ◽  
pp. 351-359 ◽  
Author(s):  
Nils-Georg Asp ◽  
Arne Dahlqvist ◽  
Otakar Koldovský
Keyword(s):  
Intestinal Mucosa ◽  
Gel Filtration ◽  
Competitive Inhibitor ◽  
The Other ◽  
Artificial Substrates ◽  
Small Intestinal Mucosa ◽  
Lactase Activity ◽  
Ph Optimum ◽  
Small Intestinal

1. Two β-galactosidases from human small-intestinal mucosa were separated by gel-filtration chromatography and the properties of the two enzymes were studied. Lactose and four hetero β-galactosides were used as substrates. 2. One of the enzymes was particle-bound and could be partially solubilized with papain. Of the substrates hydrolysed by this enzyme, lactose was hydrolysed most rapidly. This enzyme is thus essentially a disaccharidase and is named lactase. It is presumably identical with the ‘lactase 1’ described earlier. 3. The other enzyme was mainly soluble and hydrolysed all artificial substrates used, whereas no lactase activity could be detected. This enzyme has therefore been designated hetero β-galactosidase. 4. p-Chloromercuribenzoate (0·1mm) inhibited the hetero β-galactosidase completely but did not influence the activity of the lactase. Tris was a competitive inhibitor of both enzymes. 5. The residual lactase activity in the mucosa of lactose-intolerant patients may be exerted by a small amount of remaining lactase as such, or possibly by a third enzyme with a more acid pH optimum.

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