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Biomedical subjects

K A Peters

Publications and source records attributed to K A Peters.

11 recordsLinked to original sources

Relationships between the life values of U.S. college students and their cognitive/affective responses to the threat of nuclear war.

The present study was designed to examine relationships between the life values of 399 U.S. college students and their nuclear war-related thoughts, feelings, and behaviors. The students completed four scales from the Life Values Inventory: (i.e. Conventionally Defined Success [CDS]; Religious Faith and Devotion [RFD]; Activist Pursuit of Social Causes [APSC]; Materialistic Orientation [MO]), the Satisfaction With Life Scale, four scales from the Nuclear War Inventory--Nuclear Distress; Salience; Weapons Opposition; Personal Efficacy--and a single behavioral measure of approach toward information concerning nuclear weapons. Consistent with theory regarding the influence of values and commitments on attitudes and behavior, APSC was found to be positively associated with all five nuclear war measures. Additionally, MO was negatively related to Personal Efficacy and Information Approach, and CDS was positively associated with Nuclear Distress. The only value dimension which covaried significantly with general life satisfaction was RFD. Results are discussed with respect to the recent rise in conservative and materialistically-oriented values among American college students.

Adolescent

Isolation and properties of the rabbit skeletal muscle protein inhibitor of adenosine 3',5'-monophosphate dependent protein kinases.

The heat-stable protein inhibitor (Walsh, D. A., et al. (1971), J. Biol. Chem. 246, 1977--1985) of the cyclic adenosine 3',5'-monophosphate dependent protein kinase has been isolated in pure form from rabbit skeletal muscle after a 430 000-fold purification with a 47% yield. The four-step procedure involves sequentially a heat treatment, batchwise anion and cation exchange, and affinity chromatography on protein kinase catalytic subunit covalently coupled to Sepharose 4B. The inhibitor is an acidic protein (pI = 4.24) of molecular weight 11 300. It contains 98 amino acid residues none of which contains sulfur and only 2 (phenylalanine and tyrosine) are aromatic. The NH2-terminus is blocked. The muscle content is ca. 0.6 mg of inhibitor per L of intracellular water. The inhibitor is tightly bound to the catalytic subunit of protein kinase (Ki congruent to 2 X 10(-9) M) and acts competitively with respect to the protein substrates. Protein kinase recognizes a short stretch of the inhibitor sequence, in which arginyl side chains play a crucial role. A study of various competitive inhibitors of the kinase confirms the importance of guanidino groups and hydrophobic side chains in the specific interaction with the substrate binding site.

Amino Acids