|
|
||||||||
From the Department of Bacteriology and Immunology, State University of New York at Buffalo, School of Medicine, and the Millard Fillmore Hospital Research Institute, Buffalo, New York
Abstract
Prostatic acid phosphatase was demonstrated in electrophoretic patterns of prostatic fluid in the region corresponding to the serum
2- and
-globulins. In gel diffusion precipitation, this enzymatic activity was localized in two distinct bands of dense brown, speckled appearance. The titration end point of the major band varied with the sample of prostatic fluid; some were as high as 1:16000. In immunoelectrophoresis, the activity was again localized in two of the precipitin bands that were formed with the homologous antiserum. These bands were clearly of different electrophoretic mobility, suggesting that there are two different molecules having similar enzymatic properties. A number of organ extracts were tested for this phosphatase activity, namely, seminal vesicle, kidney, testicle, liver, lung and prostate gland. All of these were negative except for prostate extract, which did show one line of reaction. Normal serum was also negative. Serum from patients with carcinoma of the prostate were also positive, but only in some of the experiments. This is being further studied.
Footnotes
1 Supported in part by Research Grant CA-05499 from the National Cancer Institute, United States Public Health Service, Bethesda, Maryland.
2 Recipient of Research Career Award K6-AI-1377 from the United States Public Health Service.
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |