Metabolic mapping.

This unit describes a high-resolution [(3)H]2-deoxyglucose (2DG)/immunohistochemistry double labeling protocol which enables simultaneous visualization of metabolic and immunohistochemical markers (e.g., neurotransmitter-specific epitopes) in the same tissue section.

Evaluation of estrogen receptor immunocytochemical assay (ER-ICA) and estrogen receptor enzyme immunoassay (ER-EIA) for the determination of estrogen receptor status in breast carcinoma. A comparative study on frozen sections, cytological smears and tissue homogenates.

One hundred thirty three cases of primary breast cancer were analyzed for estrogen receptors (ERs) by two different techniques: monoclonal ER immunocytochemical assay (ER-ICA) and ER enzyme immunoassay (ER-EIA). The overall concordance between ER-ICA and ER-EIA was 89.5% despite the semiquantitative nature of the immunocytochemical evaluations.

Occurrence of the low-mobility H1 histones subfraction in embryonic, differentiated, and neoplastic tissues of the Syrian hamster.

Electrophoretically slow H1 histone subfractions with mobilities identical to that of the subfraction found in the Kirkman-Robbins hamster hepatoma chromatin have been shown to be present in 12-day hamster embryos and in a sarcoma-type hamster tumor induced by SV40. No subfractions of such mobility were found in hamster liver, regenerating liver, thymus, spleen, and a fast-growing transplantable amelanotic hamster melanoma. A suggestion is made that some defective mechanisms of differentiation may affect the regulation of expression of the genes coding for the H1 histone subfractions.

A low-electrophoretic-mobility H1 histone subfraction from Kirkman-Robbins hamster hepatoma.

A protein showing lower electrophoretic mobility in acidic urea polyacrylamide gels than did the usual histone H1 subfractions has been detected among the H1 histones extracted from chromatin of a transplantable hamster hepatoma, originally induced by Kirkman and Robbins. It was proved to be a true H1 histone subfraction. It differs from the remaining ones by the total chain length, amino acid composition, and isoelectric point value.