Isolation and partial characterization of bovine periodontal ligament alkaline phosphatase.
An alkaline phosphatase which binds to hyaluronate with a high affinity has been extracted from the bovine periodontal ligament and purified. The procedure consisted of extraction with a 10 mM Tris/Mg buffer containing 0.1% Nonidet P40, chromatography on a hyaluronate-conjugated Affi-Gel 15, and fast protein liquid chromatography. The hyaluronate-binding alkaline phosphatase has an apparent molecular weight of 110,000, contained sialic acid and was more stable to heat treatment than were two other species (Mr = 120,000 and 130,000) extracted from PDL. The heat stability and influence of inhibitors on its activity show that the hyaluronate-binding alkaline phosphatase of periodontal ligament was similar to the bone alkaline phosphatase.
Sato
S
S
Kanagawa Dental College, Japan.
Kawase
T
T
Kubota
T
T
Saito
S
S
D000469:Alkaline Phosphatase / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism; D000818:Animals; D002417:Cattle; D002846:Chromatography, Affinity; D002850:Chromatography, Gel; D002851:Chromatography, High Pressure Liquid; D004591:Electrophoresis, Polyacrylamide Gel; D016326:Extracellular Matrix Proteins / Q000737:chemistry / Q000302:isolation & purification; D006820:Hyaluronic Acid / Q000378:metabolism; D008562:Membrane Glycoproteins / Q000737:chemistry / Q000302:isolation & purification; D010513:Periodontal Ligament / Q000201:enzymology*
D016326:Extracellular Matrix Proteins; D008562:Membrane Glycoproteins; D006820:Hyaluronic Acid; D000469:Alkaline Phosphatase