title: Effect of galactose oxidase, with and without prior sialidase treatment, on the viability of erythrocytes in circulation.
abstract: Previous studies have shown that sialidase-treated mammalian erythrocytes were rapidly eliminated from circulation. In contrast, chicken asialoerythrocytes remained fully viable. This investigation was undertaken to ascertain the reason for this difference in behavior as well as to determine the extent of the similarity of the physiological mechanism for the elimination from circulation of asialoglycoproteins and mammalian asialoerythrocytes. To that end, erythrocytes from dogs, rabbits, and chickens were each subjected to the action of galactose oxidase (D-galactose:oxygen 6-oxidoreductase; EC 1.1.3.9) both before and after sialidase (acylneuraminyl hydrolase; EC 3.2.1.18) treatment. The viability of the autologously transfused erythrocytes in circulation was monitored by Na2-51CrO4 labeling. Galactose oxidase had no deleterious effect on the viability of dog or chicken erythrocytes, nor did it restore the viability of dog or rabbit asialoerythrocytes. On the other hand, desialated chicken erythrocytes, which were fully viable, were rendered nonviable upon treatment with galactose oxidase. It may be concluded therefore that (a) the physiological mechanism of elimination of mammalian asialoerythrocytes from circulation is not the same as that for plasma asialoglycoproteins and (b) the treatment of chicken asialoerythrocytes with galactose oxidase results in the oxidation at carbons 6 of the galactosyl- or N-acetylgalactosaminyl residues, thereby rendering the erythrocytes nonviable.
mesh_terms: D000818:Animals; D001786:Blood Glucose / Q000032:analysis; D002470:Cell Survival / Q000187:drug effects; D002645:Chickens; D002860:Chromium Radioisotopes; D004285:Dogs; D004912:Erythrocytes / Q000187:drug effects* / Q000201:enzymology; D005692:Galactose Oxidase / Q000494:pharmacology*; D066298:In Vitro Techniques; D000216:N-Acylneuraminate Cytidylyltransferase / Q000097:blood; D009439:Neuraminidase / Q000302:isolation & purification / Q000494:pharmacology*; D011817:Rabbits; D013045:Species Specificity; D013997:Time Factors; D014734:Vibrio cholerae / Q000201:enzymology
chemical_list: D001786:Blood Glucose; D002860:Chromium Radioisotopes; D005692:Galactose Oxidase; D000216:N-Acylneuraminate Cytidylyltransferase; D009439:Neuraminidase
references.citation: Biochem J. 1961 Nov;81:384-92
references.pmid: 13860975
references.citation: J Biol Chem. 1962 Sep;237:2736-43
references.pmid: 13863403
references.citation: Arch Biochem Biophys. 1963 Jan;100:119-30
references.pmid: 14028302
references.citation: Biochim Biophys Acta. 1957 Jun;24(3):604-11
references.pmid: 13436486
references.citation: Blood. 1975 Jan;45(1):11-20
references.pmid: 803103
references.citation: Proc Natl Acad Sci U S A. 1977 Apr;74(4):1521-4
references.pmid: 266192
references.citation: Am J Hematol. 1976;1(4):419-32
references.pmid: 1008055
references.citation: Biochem J. 1974 May;140(2):323-30
references.pmid: 4375965
references.citation: J Biol Chem. 1973 Jun 25;248(12):4311-7
references.pmid: 4711609
references.citation: J Biol Chem. 1974 Apr 10;249(7):2135-42
references.pmid: 4818830
references.citation: J Biol Chem. 1966 Dec 10;241(23):5643-50
references.pmid: 4288894
references.citation: J Biol Chem. 1965 Sep;240(9):3501-6
references.pmid: 4284295
references.citation: Adv Enzymol Relat Areas Mol Biol. 1974;41(0):99-128
references.pmid: 4609051
references.citation: Ann N Y Acad Sci. 1973 Jun 15;209:127-43
references.pmid: 4515028
references.citation: Biochim Biophys Acta. 1975 Mar 28;386(1):181-95
references.pmid: 236017
references.citation: Hoppe Seylers Z Physiol Chem. 1974 Apr;355(4):395-400
references.pmid: 4435729
references.citation: Carbohydr Res. 1974 Jun;34(2):361-9
references.pmid: 4842011
references.citation: J Neurochem. 1973 Oct;21(4):949-58
references.pmid: 4754866
references.citation: Biochim Biophys Acta. 1973 Jul 5;315(1):162-75
references.pmid: 4743899
references.citation: Proc Natl Acad Sci U S A. 1976 Feb;73(2):341-3
references.pmid: 1061137
references.citation: J Biol Chem. 1976 Jan 25;251(2):510-5
references.pmid: 1245486
references.citation: Hoppe Seylers Z Physiol Chem. 1975 Aug;356(8):1329-31
references.pmid: 1176094
references.citation: Hoppe Seylers Z Physiol Chem. 1975 Apr;356(4):391-7
references.pmid: 1150154
references.citation: Nature. 1975 Apr 24;254(5502):699-701
references.pmid: 1124129
references.citation: Biochim Biophys Acta. 1975 Mar 13;382(2):181-92
references.pmid: 1120155
references.citation: J Biol Chem. 1970 May 10;245(9):2301-8
references.pmid: 5442272
references.citation: Vox Sang. 1968;15(2):81-101
references.pmid: 5682172
references.citation: Anal Biochem. 1965 Sep;12(3):509-15
references.pmid: 5859512