The amino terminal sequence of the developmentally regulated Ch21 protein shows homology with amino terminal sequences of low molecular weight proteins binding hydrophobic molecules.
Ch21 protein, a developmentally regulated chick embryo protein of 21,000 apparent molecular weight, was purified from culture medium of hypertrophic chondrocytes. The purification method included a DEAE cellulose chromatography column, a CM cellulose chromatography column and a HPLC molecular sieve column. The amino acid sequence of the amino terminal end of the protein was determined. Computer assisted analysis showed significant homology between this sequence and the amino terminal sequences of proteins that belong to the superfamily of the low molecular weight binding proteins sharing a basic framework for the binding and transport of small hydrophobic molecules. Determination of the amino terminal sequence of the chicken retinol binding protein excluded identity between this protein and the Ch21.
Descalzi Cancedda
F
F
Istituto Nazionale per la Ricerca sul Cancro, Genoa, Italy.
Asaro
D
D
Molina
F
F
Cancedda
R
R
Caruso
C
C
Camardella
L
L
Negri
A
A
Ronchi
S
S
D000595:Amino Acid Sequence; D000818:Animals; D002352:Carrier Proteins / Q000302:isolation & purification; D002356:Cartilage / Q000032:analysis; D002645:Chickens; D002851:Chromatography, High Pressure Liquid; D002852:Chromatography, Ion Exchange; D003470:Culture Media; D004591:Electrophoresis, Polyacrylamide Gel; D008969:Molecular Sequence Data; D008970:Molecular Weight; D012689:Sequence Homology, Nucleic Acid
C020932:11-cis-retinal-binding protein; D002352:Carrier Proteins; D003470:Culture Media