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The amino acid sequence of cystatin, the protein from chicken egg-white that is a tight-binding inhibitor of many cysteine proteinases, is reported. Cystatin is composed of 116 amino acid residues, and the Mr is calculated to be 13143. No striking similarity to any other known sequence has been detected. The results of computer analysis of the sequence and c.d. spectrometry indicate that the secondary structure includes relatively little a-helix (about 20%) and that the remainder is mainly f-structure.

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One hundred and forty-eight U.S. college students from a small southwestern university were asked to provide or complete the following: the Michigan Alcoholism Screening Test (MAST), a structured alcohol-use interview, and a 10-ml blood sample to be assayed for carbohydrate-deficient transferrin (CDT) levels and gamma-glutamyl-transpeptidase (GGTP) activity. Using the data obtained in the interview, only 2 females and 5 males were identified as heavy drinkers. Conclusions regarding the efficacy of the biochemical markers are therefore limited. It was found that CDT levels were significantly and positively correlated with various measures of alcohol consumption among males. There was no similar association between CDT, or GGTP, and alcohol consumption within the female sample.

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