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Full-Text Articles in Physical Sciences and Mathematics
Inulin-125I-Tyramine, An Improved Residualizing Label For Studies On Sites Of Catabolism Of Circulating Proteins, Janet L. Maxwell, John W. Baynes, Suzanne R. Thorpe
Inulin-125I-Tyramine, An Improved Residualizing Label For Studies On Sites Of Catabolism Of Circulating Proteins, Janet L. Maxwell, John W. Baynes, Suzanne R. Thorpe
Faculty Publications
Residualizing labels for protein, such as dilactitol-125I-tyramine (125I-DLT) and cellobiitol-125I-tyramine, have been used to identify the tissue and cellular sites of catabolism of long-lived plasma proteins, such as albumin, immunoglobulins, and lipoproteins. The radioactive degradation products formed from labeled proteins are relatively large, hydrophilic, resistant to lysosomal hydrolases, and accumulate in lysosomes in the cells involved in degradation of the carrier protein. However, the gradual loss of the catabolites from cells (t1/2 approximately 2 days) has limited the usefulness of residualizing labels in studies on longer lived proteins. We describe here a higher molecular weight (Mr approximately 5000), more efficient …
Oxidative Degradation Of Glucose Adducts To Protein: Formation Of 3-(NE-Lysino)-Lactic Acid From Model Compounds And Glycated Proteins, Mahtab U. Ahmed, John A. Dunn, Michael D. Walla, Suzanne R. Thorpe, John W. Baynes
Oxidative Degradation Of Glucose Adducts To Protein: Formation Of 3-(NE-Lysino)-Lactic Acid From Model Compounds And Glycated Proteins, Mahtab U. Ahmed, John A. Dunn, Michael D. Walla, Suzanne R. Thorpe, John W. Baynes
Faculty Publications
The chemistry of Maillard or browning reactions of glycated proteins is being studied in model systems in vitro in order to characterize potential reaction pathways and products in biological systems. In previous work with the Amadori rearrangement product N alpha-formyl-N epsilon-fructoselysine (fFL), an analog of glycated lysine residues in proteins, we showed that fFL was oxidatively cleaved between C-2 and C-3 of the carbohydrate chain to yield N epsilon-carboxymethyllysine (CML) and D-erythronic acid. We then detected CML in proteins glycated in vitro, as well as in human lens proteins and collagen in vivo (Ahmed, M. U., Thorpe, S. R., and …
A Cytochemical Study Of The Transcriptional And Translational Regulation Of Nuclear Transition Protein 1 (Tp1), A Major Chromosomal Protein Of Mammalian Spermatids, Mohammad A. Heidaran, Richard M. Showman, Wilson Stephen Kistler
A Cytochemical Study Of The Transcriptional And Translational Regulation Of Nuclear Transition Protein 1 (Tp1), A Major Chromosomal Protein Of Mammalian Spermatids, Mohammad A. Heidaran, Richard M. Showman, Wilson Stephen Kistler
Faculty Publications
Immunocytochemical localization and in situ hybridization techniques were used to investigate the presence of spermatid nuclear transition protein 1 (TP1) and its mRNA during the various stages of spermatogenesis in the rat. A specific antiserum to TP1 was raised in a rabbit and used to show that TP1 is immunologically crossreactive among many mammals including humans. During spermatogenesis the protein appears in spermatids as they progress from step 12 to step 13, a period in which nuclear condensation is underway. The protein is lost during step 15. An asymmetric RNA probe generated from a TP1 cDNA clone identified TP1 mRNA …