Transglutaminase‐sensitive glutamine residues of human plasma fibronectin reveled by studying its proteolytic fragments

European Journal of Biochemistry

Volumn 154, Issue 2, 1986, Pages 371-374

  FESUS, Laszlo ^a   METSIS, Madis L ^b   MUSZBEK, Laszlo ^a   KOTELIANSKY, Victor E ^c  

^a UNIVERSITY OF DEBRECEN   (Hungary)

^b UNIVERSITY OF TARTU   (Estonia)

^c INSTITUTE OF BIOMEDICAL CHEMISTRY   (Russian Federation)

Author keywords

[No Author keywords available]

Indexed keywords

BLOOD CLOTTING FACTOR 13; FIBRONECTIN; GLUTAMINE; PEPTIDE FRAGMENT; PROTEIN GLUTAMINE GAMMA GLUTAMYLTRANSFERASE; TRYPSIN;

AFFINITY CHROMATOGRAPHY; ARTICLE; BINDING SITE; BLOOD; CATALYSIS; CHEMISTRY; HUMAN; METABOLISM;

BINDING SITES; CATALYSIS; CHEMISTRY; CHROMATOGRAPHY, AFFINITY; FACTOR XIII; FIBRONECTINS; GLUTAMINE; HUMAN; PEPTIDE FRAGMENTS; TRANSGLUTAMINASES; TRYPSIN;

EID: 0023048837     PISSN: 00142956     EISSN: 14321033     Source Type: Journal    
DOI: 10.1111/j.1432-1033.1986.tb09407.x     Document Type: Article

References (27)

1. The cell attachment domain of fibronectin. Determination of the primary structure.
2. Primary structure of human plasma fibronectin. The 29,000-dalton NH2-terminal domain.