Three new point mutations in type II procollagen (COL2A1) and identification of a fourth family with the COL2A1 Arg519-->Cys base substitution using conformation sensitive gel electrophoresis.
Williams
C J
CJ
Department of Biochemistry and Molecular Biology, Thomas Jefferson University, Philadelphia, PA 19107, USA.
Rock
M
M
Considine
E
E
McCarron
S
S
Gow
P
P
Ladda
R
R
McLain
D
D
Michels
V M
VM
Murphy
W
W
Prockop
D J
DJ
D000130:Achondroplasia / Q000235:genetics; D000595:Amino Acid Sequence; D001120:Arginine / Q000235:genetics; D001482:Base Composition; D001483:Base Sequence; D001848:Bone Diseases, Developmental / Q000235:genetics; D003545:Cysteine / Q000235:genetics; D015252:Deoxyribonucleases, Type II Site-Specific; D004591:Electrophoresis, Polyacrylamide Gel / Q000379:methods*; D005192:Family Health; D005260:Female; D006801:Humans; D007592:Joint Diseases / Q000235:genetics; D008297:Male; D008969:Molecular Sequence Data; D009690:Nucleic Acid Conformation; D010375:Pedigree; D017354:Point Mutation; D016133:Polymerase Chain Reaction; D011347:Procollagen / Q000235:genetics*; D015183:Restriction Mapping
D011347:Procollagen; D001120:Arginine; D015252:Deoxyribonucleases, Type II Site-Specific; D003545:Cysteine