Arrangement of the disulphide bridges in human low-Mr kininogen.
The arrangement of the disulphide bridges in human low-Mr kininogen has been elucidated. Low-Mr kininogen contains 18 half-cystine residues forming nine disulphide bridges. The first and the last half-cystine residues of the amino acid sequence form a disulphide loop which spans the heavy- and the light-chain portion of the kininogen molecule. The other 16 half-cystine residues are linked consecutively to form eight loops of 4-20 amino acids; these loops are lined up in the heavy-chain portion of the kininogen molecule. In this way, a particular pattern of disulphide loops is formed which seems to be of critical importance for the inhibitor function of human kininogen.
Max-Planck-Institute for Biochemistry, Martinsried, Federal Republic of Germany.
J
J
Kellermann
C
C
Thelen
F
F
Lottspeich
A
A
Henschen
R
R
Vogel
W
W
Müller-Esterl
D000595:Amino Acid Sequence; D002851:Chromatography, High Pressure Liquid; D003553:Cystine / Q000032:analysis; D004220:Disulfides / Q000032:analysis*; D007704:Kininogens; D008969:Molecular Sequence Data; D008970:Molecular Weight; D010446:Peptide Fragments / Q000032:analysis; D011487:Protein Conformation
D004220:Disulfides; D007704:Kininogens; D010446:Peptide Fragments; D003553:Cystine