Computationally Efficient Concept of Representative Directions for Anisotropic Fibrous Materials.

The concept of representative directions allows for automatic generation of multi-axial constitutive equations, starting from simplified uni-axial material models. In this paper, a modification of the concept is considered suitable for the analysis of fibrous polymeric materials, which are anisotropic in the as-received state. The modification of the concept incorporates an orientation probability density function (OPDF), which explicitly accounts for the material anisotropy.

Interaction of synthetic peptide octarphin (TPLVTLFK) with human blood lymphocytes.

The synthetic peptide octarphin (TPLVTLFK) corresponding to the sequence 12-19 of β-endorphin, a selective agonist of non-opioid β-endorphin receptor, was labeled with tritium to specific activity of 29 Ci/mmol. The analysis of [(3) H]octarphin binding to human T and B lymphocytes separated from normal human blood revealed the existence of one type of high-affinity binding sites (receptors): Kd 3.0 and 3.

Interaction of synthetic peptide octarphin with human blood lymphocytes.

The synthetic peptide octarphin (TPLVTLFK, fragment 12-19 of β-endorphin), a selective agonist of nonopioid β-endorphin receptor, was prepared with specific activity 28 Ci/mmol. The binding of [3H]octarphin to T and B lymphocytes isolated from the blood of donors was studied. It was found that [3H]octarphin binds both to T and B cells with high affinity: Kd = 3.

Synthetic peptide octarphin (TPLVTLFK) inhibits the activity of the hypothalamus-pituitary-adrenal axis through nonopioid β-endorphin receptor.

The synthetic peptide octarphin (TPLVTLFK) corresponding to the sequence 12-19 of β-endorphin, a selective agonist of nonopioid β-endorphin receptor, was labeled with tritium to specific activity of 29 Ci/mmol. The analysis of [(3)H]octarphin binding to rat pituitary and adrenal cortex membranes revealed the existence of one type of binding sites (receptors): Kd 5.9 and 35.

Interaction of the synthetic peptide octarphin with rat adrenal cortex membranes.

The synthetic peptide octarphin (TPLVTLFK, fragment 12-19 of β-endorphin), a selective agonist of the non-opioid β-endorphin receptor, was labeled with tritium yielding specific activity of 28 Ci/mmol. The binding of [3H]octarphin to rat adrenal cortex membranes was studied under normal conditions as well as after cold and heat shocks. It was found that under normal conditions [(3)H]octarphin specifically binds to the membranes with high affinity: K(d1) = 36.