The joint actions of adolescents in peer conversations about career.

Ten career conversations between adolescent peers were video-taped to examine the joint actions of adolescents that emerge in actual conversations about career. Based on an action-theoretical approach, joint action refers to the intentional behavior of a group of people attempting to realize a common goal or engage in a common process. The actual conversations and the adolescents' recall of their thoughts and feelings during the conversations were used to identify the joint actions that occurred in the conversations and the meaning that the conversations had for the adolescents. Goals of the actions included educational planning, career selection, and personal future. The functions the adolescents undertook in the conversations to reach these goals were identified as exploring, formulating, validating, and challenging. Based on these results, it was proposed that self-refinement was the project that energized and guided the joint actions and lent meaning to the conversations.

An enzyme-linked immunosorbent assay (ELISA) of denatured cartilage link protein.

Antiserum (MB007) was raised in rabbits to SDS-denatured cartilage link protein in order to develop an enzyme-linked immunosorbent assay (ELISA) to quantify link protein in cartilage extracts. The antibodies were characterized by using native and denatured link protein, either as the immobilised or the inhibiting antigen in the assay, and shown to bind more effectively to denatured link protein. At low concentrations, neither hyaluronate (0-30 micrograms/ml), proteoglycan (0-50 micrograms/ml) nor hyaluronate-binding region (0-3 micrograms/ml) competitively inhibited the link protein assay. However, at higher concentrations of proteoglycan (50 micrograms/ml-4 mg/ml) and hyaluronate-binding region (3-40 micrograms/ml) inhibition was observed. A more highly purified proteoglycan and a further purified hyaluronate-binding region preparation showed identical behaviour. The inhibition produced by proteoglycan and hyaluronate-binding region occurred at approximately equivalent molar concentrations (assuming Mr of 10(6) and 7 X 10(4), respectively). These results suggest that a significant proportion of these polyclonal antibodies recognize an epitope common to link protein and hyaluronate-binding region. However, the possibility that these effects are due to contamination with covalently bound link protein cannot be excluded. Trypsinated aggregates (0-10 micrograms/ml) produced no inhibition in the link protein ELISA, but as higher concentrations the inhibition was approximately 2000-fold lower than might have been expected from the link protein concentration present. Thus, the accessibility and/or binding of the antibodies to link protein was substantially decreased, illustrating masking of the link protein antigenic sites, as found by A. Ratcliffe and T.E. Hardingham (Biochem. J. 213 (1983) 371-378). These studies indicate that link protein in tissue extracts may be quantified in the concentration range 30-200 ng/ml and in the presence of hyaluronate, proteoglycan and hyaluronate-binding region, provided that both the immobilised and extracted link proteins are denatured.