The subunits of Concanavalin A, α-mannosidase and the main storage protein of jackbeans have been compared using the technique of peptide-mapping of iodinated tryptic peptides. The results indicate there is no structural relatedness between the lectin, enzyme and storage protein. Peptide maps of the lectin fragments which copurify with the intact subunit indicate that cleavage points additional to that between residues 118-119 most probably occur.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1007/BF00396885 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
[Vacuum ultraviolet laser dissociation and proteomic analysis of halogenated peptides].
Se Pu
February 2025
CAS Key Laboratory of Separation Sciences for Analytical Chemistry, Dalian Institute of Chemical Physics, Chinese Academy of Sciences, Dalian 116023, China.
Chemical modifications are widely used in research fields such as quantitative proteomics and interaction analyses. Chemical-modification targets can be roughly divided into four categories, including those that integrate isotope labels for quantification purposes, probe the structures of proteins through covalent labeling or cross-linking, incorporate labels to improve the ionization or dissociation of characteristic peptides in complex mixtures, and affinity-enrich various poorly abundant protein translational modifications (PTMs). A chemical modification reaction needs to be simple and efficient for use in proteomics analysis, and should be performed without any complicated process for preparing the labeling reagent.
View Article and Find Full Text PDFMultiple phosphorylated protein selective analysis via fluorous derivatization and liquid chromatography-electrospray ionization-mass spectrometry analysis.
Anal Biochem
September 2021
Faculty of Pharmaceutical Sciences, Fukuoka University, 8-19-1 Nanakuma, Johnan, Fukuoka, 814-0180, Japan. Electronic address:
Post-translational modification of proteins is involved in protein function and higher-order structure. Among such modification, phosphorylation is an important intracellular signal transduction pathway. Many studies on phosphorylated protein analysis using liquid chromatography-electrospray ionization-mass spectrometry (LC-ESI-MS) have been developed.
View Article and Find Full Text PDFCharacterization of 6-bromoferulic acid as a novel common-use matrix for matrix-assisted laser desorption/ionization time-of-flight mass spectrometry.
Rapid Commun Mass Spectrom
April 2020
Biomedical Research Center, Saitama Medical University, 38 Morohongo, Moroyama, Iruma-gun, Saitama, 350-0495, Japan.
Rationale: Ferulic acid (FA) is a standard matrix used for analyzing proteins. In this study, the ability of a halogenated FA to serve as an effective MALDI matrix was investigated. Various halogenated FAs were synthesized, and the characteristics and performance of each were compared with those of the standard matrices α-cyano-4-hydroxycinnamic acid (CHCA) and 2,5-dihydrobenzoic acid (DHBA).
View Article and Find Full Text PDFDisruption of Biofilms and Neutralization of Bacteria Using Hypochlorous Acid Solution: An In Vivo and In Vitro Evaluation.
Adv Skin Wound Care
December 2017
Anna Day, BS, is a Research Associate; Abdulnaser Alkhalil, PhD, is a Senior Research Scientist; Bonnie C. Carney, BS, is a Research Associate; Hilary N. Hoffman, BS, is a Research Associate; Lauren T. Moffatt, PhD, is the Laboratory Director; and Jeffrey W. Shupp, MD, is the Director, Firefighters' Burn and Surgical Research Laboratory, MedStar Health Research Institute, Washington, DC.
Objectives: The aims of this study were to assess the effectiveness of a hypochlorous acid-based wound cleanser (Vashe Wound Solution [VWS], SteadMed Medical, Fort Worth, Texas) in disrupting methicillin-resistant Staphylococcus aureus and Pseudomonas aeruginosa biofilms relative to other cleansers using an in vitro collagen biofilm model and to evaluate cleansers' cytotoxicity. The bioburden reduction of venous stasis wounds by VWS and another cleanser was evaluated.
Methods: Plates coated with collagen films incubated with active bacteria cultures to yield biofilm mimics were treated with VWS, 1% and 10% povidone-iodine (PI), 0.
Hormonogenic donor Tyr2522 of bovine thyroglobulin. Insight into preferential T3 formation at thyroglobulin carboxyl terminus at low iodination level.
Biochem Biophys Res Commun
July 2014
Dipartimento di Medicina e Scienze della Salute, Università del Molise, Via De Sanctis, snc, Campobasso 86100, Italy. Electronic address:
A tryptic fragment (b5TR,NR), encompassing residues 2515-2750, was isolated from a low-iodine (0.26% by mass) bovine thyroglobulin, by limited proteolysis with trypsin and preparative, continuous-elution SDS-PAGE. The fragment was digested with Asp-N endoproteinase and analyzed by reverse-phase HPLC electrospray ionization quadrupole time-of-flight mass spectrometry, revealing the formation of: 3-monoiodotyrosine and dehydroalanine from Tyr2522; 3-monoiodotyrosine from Tyr2555 and Tyr2569; 3-monoiodotyrosine and 3,5-diiodotyrosine from Tyr2748.
View Article and Find Full Text PDFWant AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!