title: Subunit structure of high molecular weight mouse nerve growth factor.
abstract: Studies from several laboratories have shown that mouse submandibular glands and mouse saliva contain nerve growth factor (NGF) as part of a high molecular weight oligomeric macromolecule composed of three different subunits, termed alpha, beta, and gamma. The beta-subunit is the nerve growth-promoting protein. The gamma-subunit is a serine protease class enzyme of highly restricted substrate specificity. The alpha-subunit has no known function. This high molecular weight form of nerve growth factor is also a Zn(II)-containing metalloprotein. In the present study, measurements of multiple physicochemical parameters have been used to deduce the subunit structure of high molecular weight NGF. Results demonstrate that it contains two alpha-, one beta- and one gamma-subunit together with one tightly bound Zn(II) ion per molecule.
mesh_terms: D000818:Animals; D001665:Binding Sites; D002851:Chromatography, High Pressure Liquid; D051379:Mice; D015394:Molecular Structure; D008970:Molecular Weight; D009414:Nerve Growth Factors / Q000302:isolation & purification; D011487:Protein Conformation; D012694:Serine; D013363:Submandibular Gland / Q000032:analysis; D015032:Zinc / Q000032:analysis
chemical_list: C013614:7S nerve growth factor complex; D009414:Nerve Growth Factors; D012694:Serine; D015032:Zinc