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At least 19 recordsLinked to original sources
PubMed1978

[Mobility on peptide maps of peptides obtained by tryptic hydrolysis of lysozyme oxidized at the S-S-bonds].

The peptide map obtained by tryptic hydrolysis of the lysozyme oxidized at the S--S-bonds was characterized and compared with that of tryptic hydrolysis of the reduced lysozyme. It was shown that the mobility of peptides containing oxidized amino acid residues is decreased under electrophoresis and chromatographic treatment. Under a decrease in the peptide charge during oxidation, the changes in electrophoretic and chromatographic mobilities show a correlation. In case when the peptide charge remains unchanged, only chromatographic mobility may be altered. It is demonstrated that the cystein residues significantly interfere with the effects of trypsin on the adjacent bonds.

Chromatography, Paper↗
PubMed1977

Structural polypeptides of Sendai virus: analysis by tryptic peptide mapping.

Tryptic peptide patterns identified Sendai virus polypeptides polypeptides HN, HN, P,F0, NP, and M as unique gene products, and confirmed the precursor-product relationship of polypeptides F0 and F. By the same criterion, the major nucleocapsid polypeptides, P and NP, in virions were derived from the same genes as their counterparts in nucleocapsids obtained from infected cells.

Culture Techniques↗
PubMedDate not supplied

[Comparative characteristics of the peptide maps of the major proteins of influenza viruses type A].

A comparative study of peptide maps of major proteins of hemagglutinin, nucleoprotein, membrane of influenza A virus strains A/WS/33, A/FM/1/47, A/Singapore/1/57, A/USSR/090/77, A/Port Chalmers/1/73 (MRC-11), was carried out. The greatest differences were observed in the peptide maps of heavy and light chains of hemagglutinin of different serotypes. The peptide maps of nucleoprotein and membrane were more similar. The A/USSR/090/77 strain by peptide maps was close to but not identical with the A/FM/1/47 strain. Structural polypeptides of the virion separated by SDS-polyacrylamide gel electrophoresis may be used satisfactorily for comparative studies of influenza virus peptide maps.

Animals↗
PubMed2025

PepMapViz: a versatile toolkit for peptide mapping, visualization, and comparative exploration.

SUMMARY: PepMapViz is a versatile R package that provides flexible peptide mapping and visualization capabilities. PepMapViz can import peptide data output from multiple popular mass spectrometry analysis tools, map peptides to their parent protein sequences, highlight protein domains and modifications, and enable comparative visualization across multiple experimental conditions. Beyond enabling visualization of MHC-presented peptide clusters in different antibody regions to predict potential immunogenicity of antibody-based therapies, PepMapViz can also aid in the visualization of cross-software mass spectrometry results at the peptide level for specific proteins, domain details in a linearized format, and post-translational modification coverage across different experimental conditions. AVAILABILITY AND IMPLEMENTATION: PepMapViz is freely available on GitHub at https://github.com/Genentech/PepMapViz and on CRAN. The package is implemented in R and includes documentation and example datasets.

Software↗
PubMed1979

Antigenic drift in type A influenza virus: peptide mapping and antigenic analysis of A/PR/8/34 (HON1) variants selected with monoclonal antibodies.

Variants of A/PR/8/34 (HON1) influenza virus, having hemagglutinin molecules with probably a single altered antigenic determinant, were isolated by growing the virus in the presence of the monoclonal hybridoma antibody PEG-1. The variants were analyzed by peptide mapping and characterized antigenically by using PEG-1 and four other monoclonal hybridoma antibodies to PR8 hemagglutinin. Peptide maps of the large hemagglutinin polypeptide, HA1, from 8 out of 10 variants showed a single changed peptide. This peptide from two of the variants was analyzed, and in each case a serine residue in the wild-type hemagglutinin was replaced by leucine in the variant. Although these eight variants showed identical peptide maps, one could be discriminated antigenically from the others with one of the hybridomas. (The peptide maps represented about one-third of the HA1 molecule.) Of the other two variants, one gave the same HA1 map as the wild type, but could be distinguished antigenically from wild-type virus by two of the hybridomas. The other was unique, and could be distinguished, both antigenically and by peptide mapping, from the other variants. Since a large number of the variants selected with PEG-1 showed the same peptide change, it is likely that this alteration in amino acid sequence (serine to leucine) was responsible for the inability of the variants to bind PEG-1 monoclonal antibody. We do not know, however, whether the changed amino acids were located within the antigenic sites or whether the change occurred somewhere else in the hemagglutinin molecule and altered the determinants through conformational changes.

Amino Acids↗
PubMed1979

Comparison of adult, embryonic, and dystrophic myosin heavy chains from chicken muscle by sodium dodecyl sulfate/polyacrylamide gel electrophoresis and peptide mapping.

Chicken myosin heavy chains from adult fast white muscle fibers (both normal and dystrophic), adult slow red fibers, and embryonic presumptive fast white fibers were compared by sodium dodecyl sulfate/polyacrylamide gel electrophoresis and by peptide mapping. The heavy chain of slow red myosin migrated electrophoretically more slowly than the heavy chains of the other myosins and differed markedly from them in its peptide maps. The heavy chain of dystrophic fast white myosin was similar to its normal counterpart by peptide mapping but showed slight differences. The peptide map of the heavy chain of embryonic presumptive fast white myosin had the general features of that of the heavy chain of fast white, not slow red, fibers but contained definite differences from the former. The results are consistent with the existence of a separate gene for the heavy chain of embryonic presumptive fast white myosin.

Animals↗
PubMed1977

Unique peptide maps of the three largest proteins specified by the flavivirus Kunjin.

Tryptic digests of four polypeptides found in Kunjin virus-infected Vero cells, NV5, NV4, V3, and NV3, were compared by peptide mapping. The polypeptides to be analyzed were labeled with radioactive methionine and separated by electrophoresis through polyacrylamide gels containing sodium dodecyl sulfate. Because infection of Vero cells by Kunjin virus does not inhibit host cell protein synthesis, radioactively labeled viral polypeptides prepared from infected cells migrate coincidentally during sodium dodecyl sulfate-gel electrophoresis with some of the labeled host proteins. Thus, the genuine viral methionine-containing peptides in tryptic digests of viral proteins have been identified by co-analyzing polypeptides from [3H]methionine-labeled uninfected cells and [35S]methionine-labeled infected cells and determining the 35S/3H ratio in the peptides resolved in two dimensions on thin-layer chromatography plates. The peptide map of NV3 demonstrated that it is host coded, whereas NV5, NV4, and V3 have unique peptide maps and, therefore, account for approximately one-half of the coding potential of Kunjin virus RNA.

Arboviruses↗
PubMed1979

Peptide mapping of heterogeneous protein samples.

A simple two-dimensional electrophoretic method for peptide mapping of heterogeneous protein samples is presented. The reduced and denatured proteins of the mixture are separated in a first dimension by sodium dodecyl sulfate-polyacrylamide slab gel electrophoresis. After completion of the electrophoresis, the whole gel lane is equilibrated in stacking gel buffer and is transferred at right angles onto a second slab gel. A protease solution is overlayed on the gel lane and a partial proteolysis of the proteins to be analyzed is performed during the stacking phase of the second electrophoresis. The second electrophoresis resolves the characteristic pattern of peptides of each individual protein as a series of spots located below the original position of the undigested protein. The peptide maps of the following samples are presented as examples: protein P23 and P23* of bacteriophage T4, membranes of Dictyostelium discoideum, membranes of human erythrocytes, and 35S-labeled proteins of D. discoideum synthesized in vivo or in a cell-free wheat germ extract. In complex samples, up to 20 individual proteins can be analyzed at once and a protein comprising only 1% of the total sample generates a clearly identifiable peptide pattern. Good reproducibility of the patterns obtained allows the comparison of samples of different origins.

Cell Membrane↗
PubMed1979

Peptide maps of the myosin isoenzymes of Acanthamoeba castellanii.

Extracts of Acanthamoeba castellanii contain four myosin-like ATPases (Maruta, H., Gadasi, H., Collins, J.H., and Korn, E.D. (1979) J. Biol. Chem. 254, 3624-3630): double-headed Acanthamoeba myosin II and single-headed Acanthamoeba myosins IA, IB, and IC, which have heavy chains of 170,000, 130,000, 125,000, and 130,000 daltons, respectively, as well as different light chains. In the accompanying paper, evidence is presented that suggests that Acanthamoeba myosin IC is the same molecule as Acanthamoeba myosin IA plus a regulatory 20,000-dalton peptide. This conclusion is confirmed by the identity of the peptide maps obtained by limited proteolysis of the heavy chains of Acanthamoeba myosins IA and IC by Staphylococcus aureus V8 protease. However, peptide maps of the heavy chains of Acanthamoeba myosins IA, IB, and II obtained by limited proteolysis by the Staphylococcus protease and chymotrypsin and by chemical cleavage by cyanogen bromide and cyanylation have few, if any, peptides in common. From this evidence, and the enzymatic and subunit data in the accompanying paper, it is concluded that the three Acanthamoeba myosin isoenzymes, IA (IC), IB, and II, are products of different genes.

Amoeba↗
PubMed1977

Comparisons of the peptide maps of Kunjin virus proteins smaller than the envelope protein.

We analyzed the maps of [35S]methionine-labeled tryptic peptides of the Kunjin virus-specified proteins NV2 1/2, NV2, V2, NV1 1/2, NV1, and V1. The peptides of NV1 1/2 are identical to those of V2, except for one peptide contained only in the latter. The maps of each of the other proteins are unique and, consequently there is no evidence of any one protein being derived from another by proteolytic cleavage. The tryptic peptide maps of the above polypeptides were also compared with those of the larger Kunjin proteins, NV5, NV4, and V3. The resolution of the peptides of NV2 1/2 and NV1 is adequate to exclude any relationships with NV5 and NV4, but a possible relationship with V3 remains, although it seems unlikely in the light of other evidence. Since the peptide map of V1 is comprised of only two methionine-containing peptides similar in mobilities to two peptides found in the maps of NV5, NV4, and V3, a precursor, if any, of V1 has not been positively identified. The peptides of NV2 and V2 (NV1 1/2) are not contained in digests of NV5, NV4, or V3, and therefore, like the latter, NV2 and V2 (NV1 1/2) are independent products of translation from the positive-strand genome.

Arboviruses↗
PubMed1979

Analytical peptide mapping by high performance liquid chromatography. Application to intestinal calcium-binding proteins.

Peptide mapping of underivatized tryptic digests of bovine and chick intestinal calcium-binding proteins has been accomplished by high performance liquid chromatography (HPLC). High precision analysis of nanomolar quantities of peptides were achieved in less than 1 h (recycle time). Peak resolution and definition are superior compared to conventional techniques and recoveries of both small (4-residue) hydrophilic and large (30-residue) hydrophobic peptides are excellent. The total amino acid composition of the bovine intestinal calcium-binding protein has been accounted for on the basis of two tryptic maps of 20 microgram of protein each.

Amino Acids↗
PubMed1979

Subunit structure and peptide mapping of junctional and extrajunctional acetylcholine receptors from rat muscle.

We have purified the junctional acetylcholine receptor from normal rat skeletal muscle and compared its structure with that of the extrajunctional receptor from denervated muscle. The two receptors from leg muscle were distinguished by isoelectric focusing and by reaction with sera from patients with myasthenia gravis. The junctional form of the acetylcholine receptor was purified from normal leg muscle by affinity chromatography on concanavalin A/Sepharose and cobrotoxin/Sepharose followed by sucrose gradient centrifugation. Analysis of radioiodinated receptor by polyacrylamide gel electrophoresis in sodium dodecyl sulfate indicated that the subunit structure of the junctional receptor was similar to that previously determined for the extra-junctional form (Froehner, S. C., et al. (1977) J. Biol. Chem. 252, 8589-8596), with major polypeptides, whose apparent molecular weights in 9% polyacrylamide gels were 45 000 and 51 000. In addition, several minor polypeptides were found. When the two receptors were labeled with different isotopes of iodine and run together on a sodium dodecyl sulfate gel, the subunits of one receptor could not be resolved from those of the other. As seen earlier with the extrajunctional form, the affinity alkylating reagent [3H]MBTA labeled the 45 000- and 49 000-dalton polypeptides of the junctional receptor. Peptide mapping showed that the two MBTA binding subunits are structurally related, although they are unrelated to the other polypeptides, and that the 45 000- and 51 000-dalton polypeptides of the junctional receptor were indistinguishable from those of the extrajunctional receptor. In addition, peptide mapping of the four subunits of acetylcholine receptor isolated from Torpedo californica electric organ showed that these four polypeptides appear to be structurally unrelated.

Acetylcholine↗
PubMed1977

Peptide mapping by limited proteolysis in sodium dodecyl sulfate and analysis by gel electrophoresis.

A rapid and convenient method for peptide mapping of proteins has been developed. The technique, which is especially suitable for analysis of proteins that have been isolated from gels containg sodium dodecyl sulfate, involves partial enzymatic proteolysis in the presence of sodium dodecyl sulfate and analysis of the cleavage products by polyacrylamide gel electrophoresis. The pattern of peptide fragments produced is characteristic of the protein substrate and the proteolytic enzyme and is highly reproducible. Several common proteases have been used including chymotrypsin, Staphylococcus aureus protease, and papain.

Alkaline Phosphatase↗
PubMed1979

Peptide maps comparing subunits of maize chloroplast and type II nuclear DNA-dependent RNA polymerases.

Both one- and two-dimensional peptide mapping techniques have been used to compare the 180-kilodalton subunits from maize chloroplast and type II nuclear DNA-dependent RNA polymerases (nucleosidetriphosphate:RNA nucleotidyltransferase, EC 2.7.7.6). Despite their similar molecular mass, these 180-kilodalton subunits are not the same. Also, two-dimensional tryptic maps of the 160-, 43-, and 28-kilodalton polypeptides from maize type II nuclear RNA polymerase and of the 140-, 42-, and 27-kilodalton polypeptides from maize chloroplast RNA polymerase show that each of these six polypeptides is unique.

Chloroplasts↗
PubMed1979

Partial N-terminal amino acid sequence analyses and comparative tryptic peptide maps of murine Ia molecules encoded by the I-A subregion.

The partial N-terminal amino acid sequences and tryptic peptide maps of I-A subregion products from the H-2b, H-2d, H-2k and H-2s haplotypes demonstrate that haplotype-associated differences are present in both alpha and beta polypeptides. The genetic and evolutionary implications of these multiple amino acid substitutions and the homology relationships among Ia molecules from human, guinea pig and the I-E subregion of the mouse are discussed.

Alleles↗
PubMed1977

Peptide mapping of 125I-labelled influenza virus proteins. Matrix proteins as markers in recombination.

We have examined the matrix proteins of A/Okuda/57, A/Finland/4/74 and A/New Jersey/8/76 viruses and several recombinant strains by radioiodination of the purified polypeptides followed by tryptic peptide mapping. The method is rapid and requires only small amounts of material. Reproducible differences were detected between the matrix proteins of the above parents and allowed origin of the matrix proteins of the recombinant viruses to be determined. The possible use of matrix protein identity as a marker in recombination work is discussed.

Chromosome Mapping↗
PubMed1977

Peptide mapping of the lambda-like chains of the BASILEA rabbits.

The recently established mutant strain of rabbits, named BASILEA, lacks the k polypeptide L-chain which is replaced by a lambda-like type (bas). This is evident from the amino acid composition and peptide maps of the bas L-chain when compared to the L-chains of the rabbits suppressed for the expression of the b locus allotypes.

Amino Acids↗