Connective tissue is considered to be composed of tightly folded polypeptide chains, resting in an extracellular amorphous ground substance consisting of polymerized muco-polysaccharides. As a result of the pioneering investigations of Meyer(1) and Duran-Reynals (2), considerable investigation has been carried out concerning alterations in composition and permeability of the ground substance in diseases affecting connective tissues (3). Alterations in the polypeptide chains responsible for the tensile strength and elasticity of connective tissue, however, have not yet been adequately studied in these diseases, nor is there any information available concerning the factors responsible for maintaining the integrity of this widely prevalent extracellular protein network. Methods suitable for clinical investigation have been lacking for investigation of this problem. We wish to report an adaptation of the hippuric acid liver function test devised by Quick (4), which has revealed in patients with active rheumatoid arthritis abnormal metabolism of at least one of the major amino acid components of collagen. These patients fail to maintain their serum glycine within 15 per cent of the fasting value after the administration of 1.77 gm. sodium benzoate intravenously.The basis for our observations rests upon the unique chemical composition of the proteins, collagen and elastin. Glycine constitutes 22.8 to 27.6 per cent by weight of these substances, accounting for approximately one-third of the total 1 Consultant, internal medicine research, Boston Regional Office, Veterans Administration; assistant Professor of Medicine, Boston University School of Medicine.2 Chief, Arthritis Clinic, Boston Regional Office, Veterans Administration.