Showing papers on "Peptide sequence published in 1968"
TL;DR: Three different but related comprehensive statistical analyses of amino acid sequences in proteins are described, to search for evidence of significant sequence structure in individual proteins relative to a purely random arrangement of the amino acid residues and to attempt to relate any significant structure uncovered to the secondary and/or tertiary configuration of the protein.
498 citations
TL;DR: Proinsulin in nearly homogeneous form has been isolated from a preparation of porcine insulin and a molecular weight close to 9100 was calculated from the amino acid composition and from sedimentation-equilibrium studies.
Abstract: Proinsulin in nearly homogeneous form has been isolated from a preparation of porcine insulin. A molecular weight close to 9100 was calculated from the amino acid composition and from sedimentation-equilibrium studies. Through the action of trypsin this single-chain protein is transformed to desalanine insulin by cleavage of a polypeptide chain connecting the carboxy-terminus of the B chain to the amino-terminus of the A chain of insulin. The amino acid sequence of this connecting peptide was found to be Arg-Arg-Glu-Ala-Gln-Asn-Pro-Gln-Ala-Gly-Ala-Val-Glu-Leu-Gly-Gly-Gly-Leu-Gly-Gly-Leu-Gln-Ala-Leu-Ala-Leu-Glu-Gly-Pro-Pro-Gln-Lys-Arg.
317 citations
TL;DR: The complete nucleotide sequence of this tRNA from Escherichia coli has been worked out and it is thought to be the chain-initiating tRNA of protein synthesis in bacterial systems.
Abstract: N-Formyl-methionyl-transfer RNA is thought to be the chain-initiating tRNA of protein synthesis in bacterial systems. The complete nucleotide sequence of this tRNA from Escherichia coli has now been worked out.
266 citations
TL;DR: The present results give the complete amino acid sequence of thioredoxin from Escherichia coli B, which contains 108 residues in a single polypeptide chain with a molecular weight of 11,657 as calculated from the sequence.
Abstract: Peptide A, the C-terminal cyanogen bromide fragment of thioredoxin, was degraded with chymotrypsin and pepsin. Partial sequences of 12 chymotryptic and 6 peptic peptides and the N-terminal tryptic peptide of trifluoro-acetylated peptide A were determined. The results were used to establish the order of the previously described tryptic peptides of peptide A and lead to the complete amino acid sequence of peptide A.
Previous experiments had established the amino acid sequence of peptide B, the N-terminal cyanogen bromide fragment of thioredoxin and the present results thus give the complete amino acid sequence of thioredoxin from Escherichia coli B. The molecule contains 108 residues in a single polypeptide chain with a molecular weight of 11,657 as calculated from the sequence. The functional group of the protein occurs in position 32 to 35 and consists of a disulfide bridge formed by two half-cystine residues separated by a glycine and a proline residue. No metals were found as part of the functional group.
259 citations
TL;DR: Molecular weight determinations of the regulatory and catalytic chains and the amino-acid sequence of the R chain indicate that the ATCase molecule contains six copies of each chain.
Abstract: Molecular weight determinations of the regulatory and catalytic chains and the amino-acid sequence of the R chain indicate that the ATCase molecule contains six copies of each chain.
249 citations
TL;DR: Within the subtilisins, there are a number of distinct repetitions of sequence; this suggests that the proteins may have evolved from shorter peptide chains by some process of extension of the sequence.
193 citations
TL;DR: It is demonstrated that caerulein is a decapeptide having the following amino acid composition and sequence: SO3H | Pyr-Gln-Asp-Tyr-Thr-Gly-Trp-Met-AsP-Phe-NH2 Synthesis has confirmed the above sequence.
180 citations
TL;DR: Phospholipase A, isolated from autolysed pancreatic tissue, appears to be identical with the product obtained by trypsin activation of the pure precursor, which has a single polypeptide chain terminating at the NH 2 region in the amino acid sequence.
178 citations
TL;DR: The complete amino acid sequence of ACP from Escherichia coli has been established in this paper, which contains 77 residues with NH2-terminal serine and COOHterminal alanine, and the pantotheine prosthetic group is attached covalently to the hydroxyl group of serine at residue 36.
167 citations
TL;DR: The complete amino-acid sequences of the alpha chains of the common genetic variants of human haptoglobin confirm that the α2 chain has arisen by partial gene duplication of the Hp1 locus, and a homology in sequence suggests that the functional similarity between haPToglobin and immunoglobin G may reflect a common evolutionary origin.
Abstract: The complete amino-acid sequences of the alpha chains of the common genetic variants of human haptoglobin confirm that the α2 chain has arisen by partial gene duplication of the Hp1 locus. A homology in sequence between a portion of the haptoglobin alpha chain sequence and a series of Bence Jones light chains suggests that the functional similarity between haptoglobin and immunoglobin G may reflect a common evolutionary origin.
139 citations
TL;DR: The complete amino acid sequence of ferredoxin from the leaves of Leucaena glauca, a species of small leguminous tree, has been determined.
TL;DR: Internal homology in cytochrome c2 of R. rubrum is demonstrated for about 83% of the molecule, suggesting evolution of this protein from a small, repeating peptide unit.
TL;DR: The complete amino acid sequence of T4 phage lysozyme is presented and the protein was found to have two cysteine residues as sulfhydryl groups in contrast to 4 S-S bridges in egg white lyso enzyme.
TL;DR: Antigenic mutants of the swine and BEL strains of influenza A virus were isolated after serial passage of these viruses in the presence of sublimiting concentrations of homologous antibody of low avidity, suggesting that antigenic variation among influenza viruses is related to changes in the amino acid sequence of their antigenic proteins.
TL;DR: It is proposed that pepsin is formed after cleavage of a glutamylisoleucyl bond between residues 41 and 42 of pepsInogen, and the amino acid composition of this segment is in excellent agreement with that estimated from the differences between the amino Acid compositions of pepinogen and peps in.
TL;DR: The complete amino acid sequence of spinach ferredoxin was determined by analyses of tryptic, chymotryptic, and thermolytic digests of various derivatives of the protein, suggesting a common archetype for plant and bacterial ferredoxins.
TL;DR: The complete amino acid sequence of Micrococcus aerogenes ferredoxin was determined with the use of the S-β-aminoethylcysteinyl (Cys(AE) derivative of the protein, and the positions of the 8 cysteine residues were found to be invariant in the three bacterial ferredoxins.
TL;DR: The peptides obtained by reaction of trypsin, pepsin, and thermolysin on the acyl carrier protein of Escherichia coli have been purified by means of ion exchange chromatography, gel filtration, and differential solubility.
TL;DR: The determination of the complete amino acid sequence of Peptostreptococcus elsdenii rubredoxin has shown that the molecule consists of a single polypeptide chain of 52 residues.
TL;DR: The molecular properties of cytochrome c2 isolated from light grown cells of the facultative photoanaerobe, Rhodospirillum rubrum, are described as evaluated after final purification by isoelectric fractionation.
TL;DR: Reduction followed by carboxymethylation of the cysteine residues with radioactive iodoacetate was found to be a powerful tool in the isolation of some insoluble peptides.
Abstract: The total amino acid sequence of a λ Bence-Jones protein has been established The protein contains 211 residues, which include two methionine residues Splitting with cyanogen bromide gave three fragments, the largest of which included the C-terminal half, which is common to other Bence-Jones proteins of the same type The peptides obtained by tryptic, chymotryptic and peptic digestion were isolated and purified by paper-electrophoretic and chromatographic techniques Reduction followed by carboxymethylation of the cysteine residues with radioactive iodoacetate was found to be a powerful tool in the isolation of some insoluble peptides Unusual features of the molecule are the fact that it contains six cysteine residues and not five as observed in both κ and λ Bence-Jones proteins studied previously, and its size, which seems two residues smaller than the smallest Bence-Jones protein studied hitherto The similarities and differences between this and other Bence-Jones proteins are discussed