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Amino Acid Residue Penultimate to the Amino-terminal Gly Residue Strongly Affects Two Cotranslational Protein Modifications, N-Myristoylation andN-Acetylation*
The amino acid residue penultimate to the N-terminal Gly residue strongly affected two cotranslational protein modifications, N-myristoylation andN-acetylation, and the amino acid requirements at this position for these two modifications were significantly affected by downstream residues.
Vertical-scanning mutagenesis of amino acids in a model N-myristoylation motif reveals the major amino-terminal sequence requirements for protein N-myristoylation.
The amino acid requirements found in this study were fully consistent with the N-terminal sequence of 78 N- myristoylated proteins in which N-myristoylation was experimentally verified and strongly indicate that the combination of amino acids at position 3, 6 and 7 is a major determinant for protein N-Myristoylations.
Effect of Polysaccharide Conjugation or Transglutaminase Treatment on the Allergenicity and Functional Properties of Soy Protein
Monitoring of polyclonal antibody titers by an indirect enzyme-linked immunosorbent assay and immunoblotting of rabbit sera, monoclonal antibody, and human allergic sera showed that soy protein−galactomannan conjugation was more effective in reducing the allergenicity of the soy protein than transglutaminase treatments and/or chymotrypsin.
A part of the transmembrane domain of pro-TNF can function as a cleavable signal sequence that generates a biologically active secretory form of TNF.
The in vitro translation/translocation assay involving a canine pancreatic microsomal membrane system including a mutant, Delta-75-47, -32-1, revealed that the N-terminal half of the transmembrane domain of pro-TNF consisting of 14 residues functioned as a cleavable signal sequence; it generated a cleaved form of TNF having a molecular mass similar to that of mature TNF.
Activation of macrophages by sulfated glycopeptides in ovomucin, yolk membrane, and chalazae in chicken eggs.
In vitro culture assay with macrophages showed that the protease digests of ovomucin, yolk membrane, and chalazae induced morphologic alteration and increased H2O2 generation and IL-1 production in lower concentration (100 micrograms/ml).
Met-Gly-Cys motif from G-protein alpha subunit cannot direct palmitoylation when fused to heterologous protein.
Heterologous fusion proteins containing the first 10 amino acids of Gi1 alpha and Gs alpha using tumor necrosis factor as a model protein determined their ability to incorporate palmitate using in vitro and in vivo expression systems and indicated the Met-Gly-Cys motif found in G-protein alpha subunits itself is not sufficient to direct palmitoylation even if Gly-2 is myristoylated after removal of initiating Met.