Six protein bands designated 1 through 6 from anode to cathode were demonstrated by agar‐gel electrophoresis of a concentrated solution of bromelin at pH 8.6 and pH 5.5. The proteolytic activity corresponded to the two most cathodal migrating bands, 5 and 6. This was the same area where sensitized erythrocyte agglutinating factor (SEAF) was located. SEAF was demonstrated only in electrophoretograms at pH 5.5 and proteolytic activity was most active at this pH. Acid phosphatase was found to be present in bands 1, 2, and 3, amylase at the point of application, peroxidase at bands 2 and 5, with an additional band lying between the point of origin and band 3. Esterase activity was present in bands 1 and 2, and PAS positive material was present in bands 4 and 5 and in a zone between the origin and band 3. From these studies it appeared that the proteolytic activity and SEAF traveled in the same portion of the electrophoretogram. Esterase, amylase and acid phosphatase activity were apparently unrelated to SEAF. Peroxidase activity and PAS positive material each were present in one of three active zones which coincided with the serologically active portion of electrophoretically separated bromelin.
Summary Anti‐bromelin antibodies prepared in rabbits were employed for immuno‐electrophoretic analysis and in serologic tests to define more clearly the property of bromelin responsible for agglutination of erythrocytes coated with incomplete antibody. The antiserum defined 9 antigenic components designated a through i. Immunoprecipitin band i had no proteolytic or peroxidase activity but appeared to correspond to an electrophoretic component of bromelin that contains both proteolytic and serologic activity. Antiserum was used to demonstrate that antigenic components of bromelin become attached to the red cell and to show that the proteolytic and the sensitized‐erythrocyte‐agglutinating factor (SEAF) of bromelin were neutralized by the anti‐bromelin antibody. Résumé Des immuns‐sérums de lapin contenant des anticorps anti‐broméline ont été préparés; ces sérums ont été utilisés pour pratiquer des analyses immunoélectrophorétiques et des tests sérologiques de façon à déterminer d'une manière plus claire la raison pour laquelle la broméline agglutine les érythrocytes revêtus d'un anticorps incomplet. L'antisérum comportait neuf composants antigéniques désignés de a à i. La ligne de précipitation i n'avait pas d'activité protéolytique ou peroxydasique, mais semblait correspondre à un composant électrophorétique de la broméline contenant l'activité protéolytique sérologique. L'immun anti‐sérum a été utilisé pour démontrer que les composants antigéniques de la broméline pouvaient s'attacher aux érythrocytes et pour démontrer également que l'action protéolytique et le facteur agglutinant de l'érythrocyte sensibilisé (sensitized‐erythrocyte‐agglutinating factor [SEAF]) de la broméline était neutralisé par l'anticorps antibroméline. Zusammenfassung Mittels Antibromelin‐Antikörpern vom Kaninchen wurden immunoelektrophoretische und serologische Untersuchungen durchgeführt, die daraufhinzielten, nähere Aufschlüsse über jene Bromelinkomponenten zu erhalten, die für die Agglutination von Erythrozyten, die mit inkompletten Antikörpern beladen sind, verantwortlich sind. Das Antiserum erfaßte 9 Antigenkomponenten, die mit den Buchstaben a bis i bezeichnet wurden. Die Präzipitationslinie i zeigte zwar selbst keine proteolytische oder Peroxydaseaktivität; sie scheint aber einer elektrophoretischen Bromelinkomponente anzugehören, die sowohl proteolytische als auch Peroxydaseaktivität aufweist. Das Antiserum wurde weiterhin zum Nachweis von Bromelinkomponenten benützt, die sich an Erythrozyten anlagern. Dabei wurde durch die Antibromelin‐antikörper die proteolytische Aktivität des Bromelins wie auch dessen Agglutinationsfaktor sensibilisierter Erythrozyten (SEAF) spezifisch gehemmt.
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