Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Antibodies against active-site peptides common to glucosyltransferases of mutans streptococci.

Infection and immunity - 1 Nov 1993

Cope P A, Mooser G

Abstract excerpt

Polyclonal antibodies were raised against peptides derived from an active-site sequence common to the family of mutans streptococcal glucosyltransferases (GTFs). The sequence contains an aspartic acid residue that functions in formation of the enzyme transition state in catalysis. Two GTFs were targeted with similar but not identical sequences in this region: one that synthesizes an alpha-1,3-linked...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Amino Acid Sequence
Share to Binding Sites
Share to Cross Reactions

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Immunoglobulin G

Share to Molecular Sequence Data

Share to Mutation

Share to Peptide Fragments

Share to Rabbits

Source

Open in PubMed Open full text

Identifiers

PMID: 8406882
DOI: 10.1128/iai.61.11.4814-4817.1993
PMCID: PMC281238

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Antibodies against active-site peptides common to glucosyltransferases of mutans streptococci.PMID 8406882Read ↗

Identification of essential amino acids in the Streptococcus mutans glucosyltransferases.Semantic proximity Read ↗

Antigenicity and immunogenicity of a synthetic peptide derived from a glucan-binding domain of mutans streptococcal glucosyltransferase.Semantic proximity Read ↗

Immunogenicity and protective immunity induced by synthetic peptides associated with a catalytic subdomain of mutans group streptococcal glucosyltransferase.Semantic proximity Read ↗

Immunogenic and protective potential of mutans streptococcal glucosyltransferase peptide constructs selected by major histocompatibility complex class II allele binding.Semantic proximity Read ↗

Glucoamylase: structure/function relationships, and protein engineering.Semantic proximity Read ↗

Engineering the glucansucrase GTFR enzyme reaction and glycosidic bond specificity: toward tailor-made polymer and oligosaccharide products.Semantic proximity Read ↗

Secondary structure of Streptococcus downei GTF-1 glucansucrase.Semantic proximity Read ↗

Proteolytic extraction enhances specific detection of the novel âSâ-type low molecular weight glutenin subunit in wheat by monoclonal antibodySemantic proximity Read ↗

Activity and thermal stability of genetically truncated forms of Aspergillus glucoamylase.Semantic proximity Read ↗

Purification of glucosyltransferases (GtfB/C and GtfD) from mutant strains of Streptococcus mutans.Semantic proximity Read ↗

Evidence that the glucoamylases and alpha-amylase secreted by Aspergillus niger are proteolytically processed products of a precursor enzyme.Semantic proximity Read ↗

Structural basis of carbohydrate transfer activity by human UDP-GalNAc: polypeptide alpha-N-acetylgalactosaminyltransferase (pp-GalNAc-T10).Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.