Single-molecule pair studies of the interactions of the α-GalNAc (Tn-antigen) form of porcine submaxillary mucin with soybean agglutinin

Biopolymers

Volumn 91, Issue 9, 2009, Pages 719-728

  Sletmoen, Marit ^a   Dam, Tarun K ^b   Gerken, Thomas A ^c   Stokke, Bjørn T ^a   Brewer, Curtis F ^b  

^a NORWEGIAN UNIVERSITY OF SCIENCE AND TECHNOLOGY   (Norway)

^b ALBERT EINSTEIN COLLEGE OF MEDICINE   (United States)

^c CASE WESTERN RESERVE UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

AFM; ConA; DFS; Lectin; Mucin; SBA

Indexed keywords

AFM; CONA; DFS; LECTIN; MUCIN; SBA; ACTIVATION BARRIERS; APPLIED FORCES; BINDING MODELS; BIOLOGICAL FUNCTIONS; DYNAMIC FORCE SPECTROSCOPY; ENERGY LANDSCAPE; GLYCOSYLATED; IMMUNE RESPONSE; LOADING RATE; LONG LIFETIME; MOLECULAR PAIRS; MOLECULAR RECOGNITION PROPERTIES; POLYPEPTIDE CHAIN; RATE OF DISSOCIATION; SINGLE-MOLECULE; SOYBEAN AGGLUTININS; UNBINDING FORCES;

ANTIGENS; ATOMIC FORCE MICROSCOPY; MOLECULAR BIOLOGY; MOLECULAR RECOGNITION; PATHOLOGY; SUGAR (SUCROSE); SUGARS; FLUORINE CONTAINING POLYMERS;

PULSE MODULATION;

AGGLUTININ; ALPHA N ACETYLGALACTOSAMINE; LECTIN; MUCIN; N ACETYLGALACTOSAMINE; UNCLASSIFIED DRUG; PLANT LECTIN; SOYBEAN LECTIN; SOYBEAN PROTEIN; TN ANTIGEN; TUMOR ANTIGEN; MICA; SOYBEAN AGGLUTININ;

ARTICLE; BINDING AFFINITY; CONTROLLED STUDY; DYNAMIC FORCE SPECTROSCOPY; FORCE; MOLECULAR RECOGNITION; NONHUMAN; PROTEIN BINDING; PROTEIN PROTEIN INTERACTION; SOYBEAN; SPECTROSCOPY; SUBMANDIBULAR GLAND; SWINE; AMINO ACID SEQUENCE; ANIMAL; ATOMIC FORCE MICROSCOPY; CHEMISTRY; GENETICS; METABOLISM; MOLECULAR GENETICS; SEQUENCE ALIGNMENT; COVALENT BOND; DISSOCIATION CONSTANT; MOLECULAR DYNAMICS; MOLECULAR INTERACTION; MOLECULAR WEIGHT; PROTEIN IMMOBILIZATION; SENSITIVITY AND SPECIFICITY; SURFACE PROPERTY;

GLYCINE MAX; SUS;

AMINO ACID SEQUENCE; ANIMALS; ANTIGENS, TUMOR-ASSOCIATED, CARBOHYDRATE; LECTINS; MICROSCOPY, ATOMIC FORCE; MOLECULAR SEQUENCE DATA; MUCINS; PLANT LECTINS; SEQUENCE ALIGNMENT; SOYBEAN PROTEINS; SUBMANDIBULAR GLAND; SWINE;

EID: 70149090833     PISSN: 00063525     EISSN: 10970282     Source Type: Journal    
DOI: 10.1002/bip.21213     Document Type: Article

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