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Objective. To investigate synovial fluid (SF) for the presence of CR1 and to study its relationship to SF leukocytes and to serum levels of soluble CR1 (sCR1) in patients with rheumatic diseases.Methods. Synovial fluids were collected from 35 patients with rheumatoid arthritis (RA) and 26 patients with other inflammatory joint diseases. Total CR1 in the SF and serum were measured with a sandwich enzymelinked immunosorbent assay (ELISA) that recognized both soluble and transmembrane forms of CR1. The characteristics of CR1 in SF were analyzed by ultracentrifugation and by a second ELISA specific for transmembrane CR1.Results. CR1 was found in all SF samples tested (range 5-281 ng/ml). SF CR1 was higher in patients with RA (mean f SD 81 -C 66 ng/ml) than in those with other inflammatory joint diseases (31.8 & 23.8 ng/ml) (P < 0.001). Serum sCRl was not significantly increased in the patients compared with the normal subjects. There was no correlation between serum sCRl and SF CR1. In 44% of the patients, the SF CR1 level was higher than the serum sCRl level. A fraction (3040%) of SF CR1 was pelleted by ultracentrifugation and, unlike serum sCR1, it reacted in an ELISA specific for transmembrane CR1. Thus, SF contained 2 forms of CRl: a membrane-associated and a soluble form, which was confirmed by sucrose density-gradient ultracentrifugation. SF CR1 levels correlated directly with the number of SF total leukocytes and polymorphonuclear

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Zusammenfassung: Aus den Keimen von Weizenund Roggensamen werden durch selektive Bindung an wasserunlösliches Trypsinharz die spezifischen Trypsininhibitoren isoliert. Es wird je l einheitlicher Inhibitor mit einem Mol.-Gew. von etwa 17000 und ein Gemisch von je 3 Inhibitoren mit Mol.-Gewichten von etwa 12000 gewonnen. Die höhermolekularen Inhibitoren bestehen aus 2 über Summary: Plant protease inhibitors, HL The purification of trypsin inhibitors from germs of wheat and rye and the localisation of the active centres.The specific trypsin inhibitors from the germs of wheat and rye were isolated by selective binding onto water-insoluble trypsin resin. One pure inhibitor, molecular weight about 17000, and a mixture of three inhibitors with molecular In der ersten Mitteilung* dieser Reihe wurde die Reindarstellung des Trypsininhibitors aus Mais-

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