Further Studies on the Mechanism of the Effect of Enzymes on Erythrocyte Serology with Special Reference to Pronase

M. D. Prager, M. L. Soules, M. A. Fletcher

Research output: Contribution to journalArticle

5 Scopus citations

Abstract

The mechanism by which pronase treatment of red cells leads to agglutination with “incomplete” antibodies has been investigated. Like other serologically active enzymes, pronase hydrolyzes arginine and lysine derivatives (the former about 100 times as readily as the latter) and releases NANA from erythrocytes in a manner which correlates with development of serologic titer. In attempting to define the minimum quantity of NANA liberation consistent with appearance of agglutination, the following quantities (μmole NANA/1010RBC) were sufficient and insufficient, respectively: for pronase, 0.28 and 0.16; for papain, 0.21 and 0.19; and for trypsin, 0.16 and 0.09. These differences may reflect differences among the enzymes with regard to producing new ionogenic groups on erythrocytes. Pronase further differed from papain and trypsin in that a minimal amount of enzyme gave no progressive NANA liberation over a six‐hour period, all of its effect being exerted by the end of 15 minutes. The utility of pronase in detection of “incomplete” Rh antibodies is excellent. 1968 AABB

Original languageEnglish (US)
Pages (from-to)220-225
Number of pages6
JournalTransfusion
Volume8
Issue number4
DOIs
StatePublished - 1968

ASJC Scopus subject areas

  • Immunology and Allergy
  • Immunology
  • Hematology

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