A membrane component of the endoplasmic reticulum that may be essential for protein translocation.
We have purified a glycosylated, membrane-spanning protein of relative molecular mass approximately 34,000 (Mr approximately 34 K) from canine microsomes that appears to be essential for protein translocation across the endoplasmic reticulum (ER) as shown by the inhibitory action of antibodies directed against it and of monovalent Fab-fragments produced from them. The ER membrane contains at least as many molecules of the 34 K membrane protein as bound ribosomes. The protein can be detected immunologically in tissues of various organisms, indicating an universal function.
Hartmann
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E
Zentralinstitut fuer Molekularbiologie der Akademie der Wissenschaften der DDR, Berlin-Buch, GDR.
Wiedmann
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M
Rapoport
T A
TA
D000818:Animals; D000906:Antibodies; D001692:Biological Transport; D015153:Blotting, Western; D004285:Dogs; D004591:Electrophoresis, Polyacrylamide Gel; D004721:Endoplasmic Reticulum / Q000378:metabolism*; D008565:Membrane Proteins / Q000302:isolation & purification* / Q000378:metabolism; D008861:Microsomes / Q000378:metabolism; D021382:Protein Sorting Signals / Q000378:metabolism*; D011506:Proteins / Q000378:metabolism*; D012261:Ribonucleoproteins / Q000302:isolation & purification; D018271:Signal Recognition Particle
D000906:Antibodies; D008565:Membrane Proteins; D021382:Protein Sorting Signals; D011506:Proteins; D012261:Ribonucleoproteins; D018271:Signal Recognition Particle