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Studies on the reproducibility of glass bead antibody affinity columns

✍ Scribed by M.E. Hodes; J.T. Glier

Publisher: Elsevier Science
Year: 1975
Tongue: English
Weight: 733 KB
Volume: 104
Category: Article
ISSN: 1873-3778
DOI: 10.1016/s0021-9673(00)91862-4

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✦ Synopsis

Rabbit antibovine spleen DNase II and antihuman parotid amylase IgG were coupled to zirconium-clad (MAO, Corning) or plain (GAO, Corning) glass beads. (These were challenged with DNase II or amylase (human parotid or pancreatic), respectively. Although columns of the beads bound the enzymes whereas control columns did not, recoveries from the immune adsorbents were not only not quantitative but extremely variable. The columns also shed material absorbing in the ultraviolet. The antiamylase IgG-MAO column bound amylase so firmly, yet without inactivating it, that an insoluble enzyme reactor was formed. For these experiments, amylase was labeled with 14C in vitro without loss of activity.

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