A novel regulatory motif at the hinge dimer interface of the MksB mediates dimerization and DNA binding activity.

The Structural Maintenance of Chromosome (SMC) protein is essential for various cellular processes, including chromosome organization, DNA repair, and genome stability. MksB, an alternative SMC protein present in prokaryotes, comprises a hinge dimerization domain and an ABC ATPase head domain linked by a coiled-coil arm. While hinge dimerization in bacterial and eukaryotic SMCs is attributed to conserved glycines, our study unveils the critical role of a novel KDDR motif located at a loop near the hinge dimer interface in Mycobacterium smegmatis MksB (MsMksB).

A site-specific phosphorylation in FSTL1 determines its promigratory role in wound healing.

Follistatin like-1 (FSTL-1) is a secreted glycoprotein of mesenchymal in origin. In human skin, FSTL1 is upregulated in the epidermal keratinocytes upon acute injury and is required for the migration of keratinocytes. Failure to upregulate FSTL1 leads to the lack of keratinocyte migration and the non-healing nature of diabetic foot ulcer (DFU).

Characterization of free oligosaccharides from garden cress seed aqueous exudate using PGC LC-MS/MS and NMR spectroscopy.

Garden cress seeds produces mucilage that has found various food applications, however, there is little information on the free oligosaccharides (FOS) contents in these seeds. Herein, we explored the presence of FOS in cress seed aqueous exudate. PGC-LC MS/MS analysis indicated the presence of mainly hexose containing oligosaccharides such as raffinose, stachyose and verbascose belonging to raffinose family of oligosaccharides (RFOs).

Discrimination of raffinose and planteose based on porous graphitic carbon chromatography in combination with mass spectrometry.

Raffinose and planteose are non-reducing, isomeric trisaccharides present in many higher plants. Structurally, they differ in the linkage of α-D-galactopyranosyl to either glucose C(6) or to C (6') of fructose, respectively and thus differentiating each other is very challenging. The negative ion mode mass spectrometric analysis is shown to distinguish planteose and raffinose.

Low-glycemic foods with wheat, barley and herbs () inhibit α-amylase, α-glucosidase and DPP-IV activity in high fat and low dose streptozotocin-induced diabetic rat.

Unlabelled: Wheat, barley or wheat + barley and herbs ( and ) based low-glycemic-index (low-GI) foods were developed and studied α-amylase, α-glucosidase and DPP-IV inhibition property in vitro and in the streptozotocin-induced diabetic rats. The GI of products ranged from 47 to 53 than control white bread (GI = 95). Total phenolic (20.

N-Glycoprofiling of immunoglobulin G and lactoferrin with site-specificity from goat milk using RP-UHPLC MS/MS.

Glycans present in glycoproteins are structurally diverse and contribute to the carbohydrate pool of the milk. Goat milk is a leading non-bovine milk source, wherein glycan diversity of several glycoproteins remains unexplored. Herein, site-specific N-glycoprofiling of two major glycoproteins - immunoglobulin G (IgG) and lactoferrin (Lf) from goat milk was performed through RP-UHPLC Q-Tof MS/MS approach.

Ameliorative effect of enhanced Fischer ratio flaxseed protein hydrolysate in combination with antioxidant micronutrients on ethanol-induced hepatic damage in a rat model.

Alcohol abuse causes severe metabolic abnormalities inducing hepatic damage and malnutrition. Since higher Fischer ratio proteins have therapeutic value in liver diseases, an investigation was undertaken to study the ameliorative effect of the enhanced Fischer ratio flaxseed protein hydrolysate (EFR-FPH) alone and in combination with antioxidant micronutrients on ethanol-induced hepatotoxicity in a rat model. The EFR-FPH was prepared by dual enzymatic hydrolysis and charcoal treatment of flaxseed protein.

Sequence and N-glycan diversity analysis of immunoglobulin G from buffalo milk using RP-UHPLC MS/MS.

Immunoglobulin G is the abundant antibody present in the colostrum and milk of major dairy animals. In the present study, buffalo milk IgG was characterized for its amino acid sequence and glycan diversity using reverse phase liquid chromatography coupled to ESI-Q-TOF MS in tandem mode. Amino acid sequence analysis of heavy chain constant region revealed the presence of two IgG subtypes namely IgG1 and IgG3, with IgG1 being the abundant.

Identification and characterization of novel transglycosylating α-glucosidase from Aspergillus neoniger.

Aim: Aspergillus niger is well established for secreting α-glucosidase having transglycosylation activity, which is used as processing aid for synthesis of isomaltooligosaccharides. The present study focuses on identification and characterization of a non-niger Aspergillus isolate and its gene conferring strong transglycosylation activity.

Methods And Results: The soil isolate was identified as Aspergillus neoniger belonging to Aspergillus section Nigri using ITS (internal transcribed spacer) and β-tubulin analysis.

Purification, characterization and specificity of a new GH family 35 galactosidase from Aspergillus awamori.

Galactosidases, ubiquitous in nature, are complex carbohydrate-active enzymes and find extensive applications in food, pharma, and biotechnology industries. The present study deals with the production of galactosidases from fungi by solid-state fermentation. Fifteen fungi were screened and Aspergillus awamori (MTCC 548), exhibited the highest α and β-galactosidase activities of 75.

Sequence characterization and N-glycoproteomics of secretory immunoglobulin A from donkey milk.

Secretory immunoglobulin A (sIgA) is the major antibody present in the human milk where it confers passive immunity to neonates. Other than human, non-ruminants such as equine, swine etc., also possess sIgA in milk but detailed characterization is limited.

Comparative Site-Specific N-Glycosylation Analysis of Lactoperoxidase from Buffalo and Goat Milk Using RP-UHPLC-MS/MS Reveals a Distinct Glycan Pattern.

The N-glycan pattern of lactoperoxidase (LPO) from buffalo and goat milk was analyzed with the corresponding site of attachment. The enzyme was purified from whey on cation exchange chromatography, proteolyzed using chymotrypsin, and the resulting (glyco)peptides were directly analyzed on reverse phase ultrahigh performance liquid chromatography coupled to ESI-Q-TOF MS in tandem mode. N-Glycans such as high mannose, complex, and hybrid types were identified in buffalo and goat LPO.

Determination of antibacterial activity and metabolite profile of against and .

Background: is one of the most used phytomedicines. To date, there is no report of determining the bioactivity of against cariogenic causing bacteria ( and ).

Objective: The objective of the present study was to determine the antibacterial activity and metabolite profile of against and .

Identification of Banana Lectin Isoforms and Differential Acetylation Through Mass Spectrometry Approaches.

Banana lectin (BanLec) exhibits specificity to glucose/mannose residues present in oligo saccharides or glycoconjugates and has attracted a lot of attention recently as a potent therapeutic agent. Structural studies and molecular cloning methods has revealed the presence of three different BanLec proteins in two species. In our study, initial mass spectrometric analysis of affinity purified native BanLec from banana pulp (Musa paradisiaca) indicated the presence of proteins with different molecular mass.

N-Glycosylation analysis of yeast Carboxypeptidase Y reveals the ultimate removal of phosphate from glycans at Asn.

Carboxypeptidase Y from Saccharomyces cerivisiae was characterized for its site specific N-glycosylation through mass spectrometry. The N-glycopeptides were derived using non specific proteases and are analysed directly on liquid chromatography coupled to ion trap mass spectrometer in tandem mode. The evaluation of glycan fragment ions and the Y ions (peptide+HexNAc) revealed the glycan sequence and the corresponding site of attachment.

Comprehensive analysis of α 2-3-linked sialic acid specific Maackia amurensis leukagglutinin reveals differentially occupied N-glycans and C-terminal processing.

Seeds of Maackia amurensis constitutes two sialic acid specific agglutinins known as leukagglutinin and hemagglutinin. Maackia amurensis leukagglutinin (MAL) recognizes α2-3-linked sialic acid present mainly in N-glycans and composed of two disulfide linked monomers. It exhibits potential N-glycosylation sites (four PNGs) which have been assumed to undergo differential occupancy.

Site specific N-glycan profiling of NeuAc(α2-6)-Gal/GalNAc-binding bark Sambucus nigra agglutinin using LC-MS revealed differential glycosylation.

The bark of Sambucus nigra contains a complex mixture of glycoproteins that are characterized as chimeric lectins known as type II ribosome inactivating proteins and holo lectins. These type II ribosome inactivating proteins possess RNA N-glycosidase activity in subunit A and lectin activity associated with subunit B exhibiting distinct sugar specificities to NeuAc(α2-6)-Gal/GalNAc and Gal/GalNAc. In the present study we have determined the N-glycosylation pattern of type II ribosome inactivating protein specific to NeuAc(α2-6)-Gal/GalNAc (Sambucus nigra agglutinin I) by subjecting it to digestion with multiple proteases.

Immuno-affinity purification of PglPGIP1, a polygalacturonase-inhibitor protein from pearl millet: studies on its inhibition of fungal polygalacturonases and role in resistance against the downy mildew pathogen.

Polygalacturonase-inhibitor proteins (PGIPs) are important plant defense proteins which modulate the activity of microbial polygalacturonases (PGs) leading to elicitor accumulation. Very few studies have been carried out towards understanding the role of PGIPs in monocot host defense. Hence, present study was taken up to characterize a native PGIP from pearl millet and understand its role in resistance against downy mildew.

N-glycan analysis of mannose/glucose specific lectin from Dolichos lablab seeds.

An affinity purified mannose/glucose specific lectin from the seeds of Dolichos lablab (Indian bean/lablab bean) resolves into five subunits upon SDS-PAGE in the range of Mr 12-20kDa. Partial de novo sequencing of subunits resulted in 88% and 73% sequence coverage for α and β subunits of the cDNA derived FRIL (Flt3 receptor interacting lectin) sequence, respectively and suggested that four bands correspond to the α-subunits while the band of lowest molecular mass is designated as β. It was proposed in an earlier study on FRIL that the difference in molecular mass of α-subunits is due to differences in C-terminal processing and differential N-glycosylation i.

Jack bean α-mannosidase: amino acid sequencing and N-glycosylation analysis of a valuable glycomics tool.

Jack bean (Canavalia ensiformis) seeds contain several biologically important proteins among which α-mannosidase (EC 3.2.1.

Characterization of α-mannosidase from Dolichos lablab seeds: partial amino acid sequencing and N-glycan analysis.

α-Mannosidase is a key enzyme in processing and degradation of N-glycans in plants and animals. In the present study α-mannosidase from crude extracts of Dolichos lablab (Indian beans) has been purified by ammonium sulfate precipitation, anion exchange, galactose Sepharose, phenyl Sepharose, gel permeation and Con A Sepharose chromatography. The purified protein migrated as a single band corresponding to 116 kDa on SDS-PAGE under reducing conditions.