The isolation and primary structure of a 22-kDa extracellular matrix protein from bovine skin.
The primary structure of a 22-kDa protein which was isolated during the purification of bovine skin dermatan sulfate proteoglycan is described. The uronate-rich fraction from DEAE-Sepharose chromatography of a 7.8 M urea extract of bovine fetal skin was subjected to gel filtration on Sepharose CL-6B in 4 M guanidine HCl. A prominent component of mass 22 kDa was separated from the proteoglycan and further purified on octyl-Sepharose. The primary structure of this component was determined and found to contain three repeat regions. Each of the three sections contains a similar pattern of looped disulfide bonds. A six-amino acid consensus sequence, Asp-Arg-Glx-Trp-Asn/Gln/Lys-Phe/Tyr, is found in each loop. This domain may be involved in associations of the molecule with other extracellular matrix components.
Neame
P J
PJ
Shriners Hospital for Crippled Children, Tampa Unit, Florida.
Choi
H U
HU
Rosenberg
L C
LC
D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D002807:Chondroitin / Q000031:analogs & derivatives*; D011508:Chondroitin Sulfate Proteoglycans / Q000302:isolation & purification*; D002850:Chromatography, Gel; D002851:Chromatography, High Pressure Liquid; D002852:Chromatography, Ion Exchange; D003871:Dermatan Sulfate / Q000302:isolation & purification*; D005109:Extracellular Matrix / Q000032:analysis*; D005333:Fetus; D008969:Molecular Sequence Data; D008970:Molecular Weight; D011487:Protein Conformation; D011509:Proteoglycans / Q000302:isolation & purification*; D012867:Skin / Q000032:analysis*
D011508:Chondroitin Sulfate Proteoglycans; D011509:Proteoglycans; C032649:dermatan sulfate proteoglycan; D003871:Dermatan Sulfate; D002807:Chondroitin