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The SHS is a valid, reliable and responsive measure of subjective health in patients with ulcerative colitis. It is simple to administer, quickly completed and the results do not need further calculations. The SHS can be used in clinical trials and in clinical practice to identify the patient's main problems affecting health.

To correctly interpret health-related quality of life assessments, it is necessary to consider co-morbidity and gender distribution in addition to the symptom burden of the disease studied.

Factor B of the alternate pathway participates in the activation of complement component C3. Factor B and fragments thereof have been isolated from serum and partially characterized. Highly purified factor B is homogeneous by agarose electrophoresis but electrophoretic techniques with higher resolution and isoelectric focusing reveal two types of charge heterogeneity for factor B. The heterogeneity is thus partly dependent upon a genetic polymorphism but in addition a nongenetical microheterogeneity is observed. The sedimentation constant for factor B is 5.9 S and the Stokes' molecular radius is 40 A. The molecular weight of factor B was assessed by several techniques and a value of about 90 000 was established with all methods. These data demonstrated that factor B consists of a single polypeptide chain. The "1-terminal amino acid residue was shown to be proline. Factor B contains about 7.3% carbohydrate. Two fragments of factor B were also encountered in serum. The quantitatively dominating component had a molecular weight of 63 000, was basic in character, and did not exhibit any high degree of charge heterogeneity. Occasionally a basic fragment with the molecular weight 47 000 was also obtained. Immunological analyses revealed that both fragments displayed less antigenic sites than A key step in the complement reaction sequence is the activation of C3 (see Muller-Eberhard, 1975). This can occur principally in two ways. The classical activation mechanism involves factors C1, C4, and C2 but an alternate pathway is also existent. Factors A, B, and D can accordingly participate in the formation of a C3 convertase (for a review, see MullerEberhard, 1971). Factor B (C3 proactivator) was first isolated by Gotze and Muller-Eberhard (1 971). They estimated the molecular weight of factor B to 80 000 and showed that on activation the protein lost an acidic fragment with an apparent molecular weight of about 20 000 leaving the C3-cleaving activity associated with a basic polypeptide with the molecular weight 60 000. Haupt and Heide (1965) and Boenish and Alper (1970a) isolated independently a serum glycoprotein with @l to y mobility on electrophoresis. The latter authors noted that the isolated protein probably represented a fragment of a larger glycoprotein, which subsequently was successfully isolated (Boenish and Alper, 1970b). This protein, termed glycine-rich 0-glycoprotein, was shown to display two major electrophoretic forms, S and F, which strongly indicated a genetically controlled polymorphism in the glycine-rich P-glycoprotein (Alper et al., 1972). In addition several minor, nongenetically deter-

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