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"Western blotting": electrophoretic transfer of proteins from sodium dodecyl sulfate--polyacrylamide gels to unmodified nitrocellulose and radiographic detection with antibody and radioiodinated protein A.
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Microprocedures for quantitative immunochemical analysis of antigenic molecules and antigenic determinants.
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Translocation of proteins across the endoplasmic reticulum III. Signal recognition protein (SRP) causes signal sequence-dependent and site-specific arrest of chain elongation that is released by microsomal membranes.
J Cell Biol. 1981 Nov;91(2 Pt 1):557-61
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Protein translocation across the endoplasmic reticulum. I. Detection in the microsomal membrane of a receptor for the signal recognition particle.
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Protein translocation across the endoplasmic reticulum. II. Isolation and characterization of the signal recognition particle receptor.
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Subcellular distribution of signal recognition particle and 7SL-RNA determined with polypeptide-specific antibodies and complementary DNA probe.
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Signal recognition particle: a ribonucleoprotein required for cotranslational translocation of proteins, isolation and properties.
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Xenopus oocytes can secrete bacterial beta-lactamase.
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Electroblotting of multiple gels: a simple apparatus without buffer tank for rapid transfer of proteins from polyacrylamide to nitrocellulose.
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Purification of microsomal signal peptidase as a complex.
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Protein translocation across and integration into membranes.
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The signal sequence of nascent preprolactin interacts with the 54K polypeptide of the signal recognition particle.
Nature. 1986 Apr 17-23;320(6063):634-6
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The signal recognition particle receptor is a complex that contains two distinct polypeptide chains.
J Cell Biol. 1986 Oct;103(4):1167-78
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Photocrosslinking of the signal sequence of nascent preprolactin to the 54-kilodalton polypeptide of the signal recognition particle.
Proc Natl Acad Sci U S A. 1986 Nov;83(22):8604-8
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Direct probing of the interaction between the signal sequence of nascent preprolactin and the signal recognition particle by specific cross-linking.
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A signal sequence receptor in the endoplasmic reticulum membrane.
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Growth phase-dependent proteins of the Ehrlich ascites tumor analyzed by one- and two-dimensional electrophoresis.
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Protein measurement with the Folin phenol reagent.
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Cleavage of structural proteins during the assembly of the head of bacteriophage T4.
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A rapid, sensitive, and specific method for the determination of protein in dilute solution.
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High resolution two-dimensional electrophoresis of proteins.
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Identification and characterization of a membrane component essential for the translocation of nascent proteins across the membrane of the endoplasmic reticulum.
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