Amino Acid Sequence Of Subunit Research Articles

Is the mitochondrially made subunit 2 of cytochrome oxidase synthesized as a precursor in Neurospora crassa?

Amino acid sequencing of subunits of cytochrome oxidase from beef heart has revealed that the mitochondrially made subunit II of the enzyme starts with formyl-methionine at the amino terminus [ 11. This result is consistent with the identification of N-formyl-methionine as a residue present in nascent polypeptides, as well as in ‘intrinsic’ membrane proteins of yeast mitochondria [2,3]. No information is available indicating that, similar to bacteria, a post-translational removal of the formyl residues, or/and a subsequent processing of the amino ends of the polypeptide chains takes place in mitochondria prior to the integration into functional membrane complexes. We have obtained strong evidence, both from kinetic experiments [4] and from amino acid sequence data (W.M., S.W., in preparation) that the mitochondrially synthesized subunit 1 of the Neurospora oxidase is formed from a larger precursor polypeptide extended at the amino terminus. Here we present the partial N-terminal sequence of subunit 2 of the Neurospora enzyme suggesting the existence of a

Amino acid sequence of subunit V of bovine heart cytochrome oxidase, the heme alpha-containing subunit.

The complete amino acid sequence of the heme alpha-containing subunit V of bovine heart cytochrome oxidase was determined to be: H2N-Ser-His-Gly-Ser-His-Glu-Thr-Asp-Glu-Glu-Phe-Asp-Ala-Arg-Trp-Val-Thr-Tyr-Phe-Asn-Lys-Pro-Asp-Ile-Asp-Ala-Trp-Glu-Leu-Arg-Lys-Gly-Met-Asn-Thr-Leu-Val-Gly-Tyr-Asp-Leu-Val-Pro-Glu-Pro-Lys-Ile-Ile-Asp-Ala-Ala-Leu-Arg-Ala-Cys-Arg-Arg-Leu-Asn-Asp-Phe-Ala-Ser-Ala-Val-Arg-Ile-Leu-Glu-Val-Val-Lys-Asp-Lys-Ala-Gly-Pro-His-Lys-Glu-Ile-Tyr-Pro-Tyr-Val-Ile-Gln-Glu-Leu-Arg-Pro-Thr-Leu-Asn-Glu-Leu-Gly-Ile-Ser-Thr-Pro-Glu-Glu-Leu-Gly-Leu-Asp-Lys-Val-COOH. The subunit V is a single polypeptide which consists of 109 amino acid residues. The protein contains 48.6% hydrophobic residues and 34.0% hydrophilic residues and it is an acidic protein having a net charge of -3 at neutral pH. The molecular weight of subunit V was calculated to be 12,436 and that for the heme alpha-containing polypeptide was 13,295.

Mass spectrometric sequencing of proteins. The structure of subunit I of monellin

The amino acid sequence of subunit I of the sweet protein monellin has been completed by gas chromatographic mass spectrometry. A partial acid hydrolyzate was converted to the corresponding mixture of N ω-trifluoroethyl-polyamino alcohol-trimethylsilyl ethers and a total of 55 di- to hexapeptides were identified which could be assembled to a polypeptide chain of 44 amino acids.

Chymotryptic inhibitor I from potatoes: The amino acid sequences of subunits B, C and D

FEBS LettersVolume 45, Issue 1-2 p. 11-13 Full-length articleFree Access Chymotryptic inhibitor I from potatoes: The amino acid sequences of subunits B, C and D M. Richardson, M. Richardson Department of Botany, University of Durham, Durham DH1 3LE, EnglandSearch for more papers by this authorL. Cossins, L. Cossins Department of Botany, University of Durham, Durham DH1 3LE, EnglandSearch for more papers by this author M. Richardson, M. Richardson Department of Botany, University of Durham, Durham DH1 3LE, EnglandSearch for more papers by this authorL. Cossins, L. Cossins Department of Botany, University of Durham, Durham DH1 3LE, EnglandSearch for more papers by this author First published: September 01, 1974 https://doi.org/10.1016/0014-5793(74)80798-2Citations: 42AboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL Share a linkShare onFacebookTwitterLinked InRedditWechat No abstract is available for this article.Citing Literature Volume45, Issue1-2September 01, 1974Pages 11-13 ReferencesRelatedInformation

Chymotryptic inhibitor I from potatoes. The amino acid sequence of subunit A*

The amino acid sequence of subunit A of the potato chymotryptic inhibitor I was determined. The sequence was deduced from analysis of fragments and peptides derived from the protein by cleavage with cyanogen bromide, N-bromosuccinimide and dilute acid, and by digestion with trypsin, thermolysin, pepsin and papain. The molecule consists of a single polypeptide chain of 84 residues, which contains two homologous regions each of 13 amino acids. The protein does not appear to be homologous with any other known proteinase inhibitors.