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Abstract
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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Article info
Publication history
Accepted:
October 1,
1968
Received:
September 3,
1968
Footnotes
☆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.
Identification
Copyright
© 1969 Published by Elsevier Inc.