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The development of a 16-item nutritional risk index (NRI) is chronicled from its inception through its application in three studies designed to assess its reliability and validity. Study I involved a survey of 401 community-dwelling elderly in St. Louis, Missouri who were interviewed at baseline, 4-5 mo later, and 1 yr later. Study II involved a cross-sectional survey of 377 male outpatients attending two clinics at the St. Louis Veterans Administration Medical Center. Study III involved a cross-sectional survey of 424 community-dwelling elderly in Houston, Texas. Internal consistency reliability coefficients ranged between 0.47 and 0.60, and test-retest reliability coefficients ranged between 0.65 and 0.71. Validity was established by using the NRI to predict the use of health services, as well as by correlating it with a variety of anthropometric, laboratory, and clinical markers of nutritional status. The utility of the NRI for future applications is discussed.

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Blood protein concentrates were prepared from the serum and decolorized hemoglobin fractions of bovine blood. The emulsifying capacity of the concentrates was dependent on protein concentration and was not affected by spray drying. However, when the serum protein fraction was subjected to the decolorization treatment, its emulsifying capacity was reduced. Lactose, when added to the serum proteins prior to spray drying, prevented this reduction.

The control (C) side of 23 animals was placed in a 2°C chill room at 1 hr postmortem, while the other side was high temperature cdnditioned (HT) at approximately 22°C for 4 hr postmortem, at 12°C for an additional 8 hr and was then placed in the 2°C chill room. The activity of cathepsin C and fl-glucuronidase was measured on the nuclear, micro: somal, and unsedimentable fractions at 12, 18 and 24 hr postmortem in order to determine the amount of sedimentable and free enzyme activity at these postmortem times. High temperature conditioning enhances the disruption of the lysosomal membrane as evidenced by a significant increase in percent of free enzyme activity at 12 hr postmortem for both cathepsin C and pglucuronidase. There was also a significant decrease in total activity for both enzymes of the HT group at 12 hr postmortem due to autolysis of the free enzyme. These differences were not present at 18 and 24 hr postmortem (except for decreased total activity of cathepsin C at 18 hr), indicating that differences caused by high temperature conditioning take place very early postmortem and that the differences in enzyme activities are not detectable at later postmortem times These results indicate that some of the differences in tenderness produced by HT treatments are possibly associated with the increased level of free lysosomal enzymes during the first 12 hr postmortem.

Some precursors of beef flavor have been investigated. Those dealt with here appear to be relatively simple water-soluble components of beef muscle tissue. Inosinic acid or inosine and inorganic phosphate have been identified as one of the compounds involved. A glycoprotein of unknown structure is another component. Glucose has been identified as the sugar moiety of the glycoprotein. The amino acid composition is also discussed.