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Application of a microchemical technique to the elucidation of enzyme activity profiles within single human mammary tumors
Author(s) -
Larner Elizabeth H.,
Rutherford Charles L.
Publication year - 1978
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(197805)41:5<1863::aid-cncr2820410530>3.0.co;2-t
Subject(s) - malate dehydrogenase , aldolase a , glucose 6 phosphate isomerase , lactate dehydrogenase , hexokinase , pyruvate kinase , enzyme , dehydrogenase , biochemistry , phosphofructokinase , fructose bisphosphate aldolase , lactate dehydrogenase a , glycolysis , biology , microbiology and biotechnology , chemistry
An ultramicrochemical technique has been adapted to the evolution of enzyme profiles within individual human mammary tumors. Tandem observation of adjacent stained and lyophilized sections permitted dissection of microgram quantities of freeze‐dried material within confirmed regions of malignancy. Enzymes frequently monitored to examine glycolytic, respiratory, and metastatic capacity were microanalyzed successfully: lactic dehydrogenase (LDH), phosphoglucose isomerase (PGI)malate dehydrogenase (MDH), acid phosphatase (AP), aldolase (ALD), glucose‐6‐phosphate dehydrogenase (G6PDH), pyruvate kinase (PK), α‐glycerophosphate dehydrogenase (α‐GOPDH), hexokinase (HK), and phosphofructokinase (PFK). All enzyme activities were higher in infiltrating ductal carcinomas than in fibroadenomas. Extracts of tumor cells mixed in varying proportions with brain or muscle extracts of rat evidenced no modification of expected activity. The technical adaptation described provided a sensitive methodology to resolve problems of replication, profile analysis, sample quantity, and selectivity within heterogeneous tissues.