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Establishment of the integrity of lysosomes in a glycoprotein-rich matrix:Distribution pattern of seven lysosomal enzymes in gastric mucosa

Authors
Journal
Biochimica et Biophysica Acta (BBA) - General Subjects
0304-4165
Publisher
Elsevier
Publication Date
Volume
444
Issue
2
Identifiers
DOI: 10.1016/0304-4165(76)90394-9
Disciplines
  • Biology

Abstract

Abstract Gel-forming mucosal glycoproteins strongly interfere with standard methods of cell fractionation. Thus, acid hydrolase-bound particles imbedded in the gel, sediment on centrifugation, in the nuclear fraction of homogenates of canine antral mucosa. These particles can be cleared by direct solubilization of the gel; however, the viscosity of the solution obtained prevents sedimentation of some of the latent hydrolases, even at very high speeds. The use of a new step-wise scheme of centrifugation and dilution successfully isolates lysosomal particles containing acid hydrolases from mucin-rich mucosa. All of the enzymes investigated, including acid phosphatase, cathepsin D, α- and β-galactoside, β- N-acetylhexosaminisides, but with the exception of α-fucosidase, were found to be particle bound, exhibiting high degrees of latency. However, active mucosal particles are polydisperse in size and density, sedimenting under different centrifugal forces.

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