Publications by authors named "LITMAN R"
Article Synopsis
- The heavy chains from three monoclonal IgG1 cryoimmunoglobulins showed different mobility in SDS-PAGE compared to noncryoglobulin references, but this did not align with their ability to precipitate.
- High sensitivity gel filtration indicated that their molecular weights were similar to noncryoglobulins, ruling out significant differences there.
- The unique electrophoretic mobility may stem from distinct structures or charges of the SDS-protein complexes, particularly in their Fd portions, as it’s the only shared abnormality among the cryoimmunoglobulins.
Article Synopsis
- Calcium trapped in bovine rod outer segment disks releases approximately 0.75 calcium ions for each rhodopsin molecule that is bleached when exposed to light, with the release being proportional to the degree of bleaching.
- The study utilizes a flow system to monitor calcium release, showing that while trapped calcium levels don't affect release rates, previous exposure to a calcium ionophore prevents light-triggered calcium efflux, indicating calcium is released from within the disks, not the external surface.
- Lowering the temperature suppresses calcium release, suggesting that a structural change occurs in the rhodopsin after bleaching that facilitates calcium transport, leading to the concept that each bleached rhodopsin functions as a "one-shot carrier" for calcium ions
Human erythrocytes have been used as a model for evaluating the chemical carcinogen-plasma membrane interaction. The carcinogenic aromatic amines 2-acetylaminofluorene, dimethylaminoazobenzene, and 3'-methyldimethylaminoazobene stabilize erythrocytes against lysis in hypotonic solution. In general, the stabilization potential of these compounds reflects their oil:water partition coefficients and may be related to both their extracellular distribution and ultimate capacity for penetration of target cells.
View Article and Find Full Text PDFAnalysis of polypeptide disposition in human erythrocyte membranes employing membrane inversion.
Biochim Biophys Acta
July 1975
High resolution segregation of erythrocyte membrane polypeptides achieved by isoelectric focusing in 8 M urea was employed in conjunction with surface-restricted radioiodination to analyze the disposition of polypeptides within the human erythrocyte membrane. Several membrane polypeptides showed significant uptake of radioiodine, with the principal labeled component migrating between pH values of 3.0 and 3.
View Article and Find Full Text PDFAn unusual exonuclease activity associated with Micrococcus luteus DNA polymerase.
Biochem Biophys Res Commun
October 1970