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Acid phosphatase in human breast cancer tissue
Author(s) -
Filmus Jorge E.,
Podhajcer Osvaldo L.,
Mareso Eduardo,
Guman Natalio,
Mordoh José
Publication year - 1984
Publication title -
cancer
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.052
H-Index - 304
eISSN - 1097-0142
pISSN - 0008-543X
DOI - 10.1002/1097-0142(19840115)53:2<301::aid-cncr2820530220>3.0.co;2-3
Subject(s) - isozyme , antiserum , sephadex , acid phosphatase , counterimmunoelectrophoresis , mammary gland , microbiology and biotechnology , enzyme , biology , pathology , biochemistry , medicine , cancer , breast cancer , immunology , antibody
When the total acid phosphatase (AP) activity of mammary carcinoma was compared with those of benign pathology and normal mammary tissue the results showed statistically significant differences ( P < 0.05) when expressed per milligram of protein: 358 ± 42 nmoles per hour (mean ± standard error) in the malignant tumor, 216 ± 30 in the benign pathology, and 96 ± 45 in normal tissue and when expressed per milligram of DNA: 1858 ± 234, 1227 ± 140, 695 ± 345 nmoles per hour, respectively. The polyacrylamide gel electrophoretic profiles showed different levels of isoenzymes 3 and 4 in the three tissue groups. The appearance of isoenzyme 1 is reported after treatment of the homogenates with 5% Triton X‐100. It was also found by counterimmunoelectrophoresis that the 28,000 Xg mammary tumor supernatant cross reacts with an antiserum raised against AP isoenzyme 2 although the mammary tissue does not contain such an isoenzyme. To elucidate this point, isoenzymes 1, 3 and 4 were separated by columns of Sephadex G‐200 and DEAE‐Sephadex. By counterimmunoelectrophoresis, it was observed that only the fraction containing isoenzyme 4 cross‐reacted with the antiserum anti‐AP isoenzyme 2 maintaining the catalytic activity.