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Vectorial Pansport of Proteins into and across Membranes by Alan M. Tartakoff (Eds.)

24 February 2017 adminNonfiction 3

By Alan M. Tartakoff (Eds.)

This is often the 3rd quantity during this sequence overlaying protein translocation inside of and among cells. Volumes 31 and 32, Vesicular delivery, elements A and B, taken care of options for eukaryotic cells on hand as of 1989. This quantity, Vectorial shipping of Proteins into and throughout Membranes, brings jointly new equipment and new subject matters as of 1991. Highlights comprise use of anti-idiotype antibodies, gene fusions, transcription, crosslinking, pulse-labeling, and reconstitution. Key positive aspects* Describes modern ways for learning* Protein delivery* Protein topology* Organelle biogenesis* Covers equipment from pre-eminent laboratories together with* In vitro and in vivo investigations* Biochemical and immunological thoughts* Prokaryote, chloroplast, mitochondria, peroxisome, and tough endoplasmic reticulum membranes

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Extra info for Vectorial Pansport of Proteins into and across Membranes

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Virus budding occurs at the plasma membrane of the infected cell and results in the enclosure of the nucleocapsid within a layer of viral glycoproteins embedded in a host cell-derived lipid bilayer (Fig. 10) (Simons and Garoff, 1980). Host cell membrane proteins are almost completely excluded from this forming envelope, and considerable interest has focused on the sorting mechanism responsible for this effect. A specific interaction between the cytoplasmic domains of the spike glycoprotein complex and the surface of the nucleocapsid was proposed by Simons and Garoff (1980), supported by the results of crosslinking experiments (Garoff and Simons, 1974).

1988). The unconjugated 31-residue synthetic peptide was found to be strongly immunogenic in BALB/c mice, giving rise to antibodies that recognized the peptide and the whole E2 molecule both by immunoprecipitation and immunofluorescence on permeabilized infected cells. After paired in vicru immunization, hybridomas was selected for their ability to label infected but not uninfected cells. From 110 wells containing hybridomas, 5 wells were obtained that showed this ability; all gave similar staining patterns in infected cells.

R. B. (1990). The retention signal for soluble proteins of the endoplasmic reticulum. Trends Biochem. Sci. 15, 483-486. Perelson, A. S. (1989). Immune network theory. Immunol. Rev. 110, 5-36. Reading, C. L. (1982). Theory and methods for immunization in culture and monoclonal antibody production. J . Immuno. Methods 53, 261-291. Rose, J. , and Doms, R. W. (1988). Regulation of protein export from the endoplasmic reticulum. Annu. Rev. Cell Biol. 4, 257-288. Roth, M. , and Pierce, S. B. (1987). In vivo crosslinking of protein disuphide isomerase to immunoglobulins.

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