Premium
Electrophoretic analysis of glycoprotein enzymes in the sialidoses and mucolipidoses
Author(s) -
SWALLOW D. M.,
O'BRIEN J. S.,
HOOGEVEEN A. T.,
BUCK D. W.
Publication year - 1981
Publication title -
annals of human genetics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.537
H-Index - 77
eISSN - 1469-1809
pISSN - 0003-4800
DOI - 10.1111/j.1469-1809.1981.tb00303.x
Subject(s) - isoelectric focusing , alkaline phosphatase , enzyme , sialidase , acid phosphatase , neuraminidase , biochemistry , glycoprotein , electrophoresis , isoelectric point , microbiology and biotechnology , chemistry , mucolipidosis , isozyme , biology
SUMMARY Ten enzymes, all known to be glycoproteins, were examined by electrophoresis or gel isoelectric focusing in 12 different patients with primary or secondary sialidase deficiency. Aberrant electrophoretic mobilities of many of the enzymes attributable to abnormal sialylation were found in all the patients. In ten of the patients seven of the enzymes were affected. The unaffected enzymes were β ‐galactosidase, alkaline phosphatase and β ‐glucuronidase. In the cells from the two patients with I cell disease (mucolipidosis II) in which sialidase is one of many deficient enzymes, β ‐galactosidase, α ‐galactosidase, α ‐fucosidase and α ‐mannosidase were undetectable, alkaline phosphatase showed a normal electrophoretic mobility and acid phosphatase, adenosine deaminase, α ‐glucosidase and β ‐D‐ N ‐acetylhexosaminidase showed aberrant mobilities.