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Human leukocytes show α-glucosidase activity with maltose as substrate and β-galactosidase activity with 6-bromo-2-napthyl-β-galactopyranoside as substrate. There was no detectable activity of sucrase, isomaltase, or lactase in human leukocytes. By glass bead columns, the white blood cells were separated into pure lymphocytes and pure polymorphonuclear leukocytes. β-galactosidase and maltase were present in about equal proportions in the two pure cell fractions. By investigating the pH optimum, heat inactivation, Km, and intracellular distribution following ultracentrifugal separation, the β-galactosidase in leukocytes is similar to that seen in liver and probably the soluble fraction in the intestine and represents a lysosomal enzyme. There was no evidence of different β-galactosidases at pH 3.5 and 5.5 in leukocytes. The α-glucosidase in leukocytes is resistant to heat inactivation at 54 °C. and partially resistant to heat inactivation at 64 ° C. The presence of maltase and absence of sucrase and isomaltase together with heat inactivation characteristics suggest that the maltase present in leukocytes is in the form of maltase I and II or maltase 1+2. It appears not improbable that this maltase complex is made up of two or more different α-glucosidases. One of thes appears to be lysosomal in nature as shown by the intracellular distribution at pH 4.0. These observations indicate that the disaccharidases located in the brush border region of the intestinal mucosa are not present in white cells. However, the β-galactosidase and at least one of the α-glucosidases observed in leukocytes probably represent lysosomal enzymes.
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Accepted: October 1, 1968
Received: September 3, 1968
☆These studies were aided by grants from the Otho S. A. Sprague Institute, the Illinois Mental Health Fund, and the National Institutes of Health Grants T1-AM-5186, T1-HD-36, and 1-S01-FR-5475.
© 1969 Published by Elsevier Inc.