Abstract: A method for treating a patient having a wound is described. The method includes administering an amount of a chemodenervating agent such that healing of the wound is enhanced. The method is illustrated by detailing the mean differences of the scores of the paired experimental and control scars across three observers.

Abstract: A method for treating a patient having a wound is described. The method includes administering an amount of a chemodenervating agent such that healing of the wound is enhanced. The method is illustrated by detailing the mean differences of the scores of the paired experimental and control scars across three observers.

Abstract: The invention provides methods and materials related to the diagnosis of eosinophil degranulating conditions. Specifically, the invention provides methods and materials that involve visual types of analysis (e.g., microscopic analysis) that are used to determine the presence or absence of a horseshoe-shaped eosinophil granule structure within a mucus sample collected from a mammal. The presence of a horseshoe-shaped eosinophil granule structure within a patient's mucus indicates that the patient has an eosinophil degranulating condition. In addition, the invention provides methods and materials that involve immunological types of analysis (e.g., immunoassays) that are used to determine if a patient's mucus contains a tissue-damaging amount of eosinophil granule content that is outside the eosinophil granule and within the mucus.

Abstract: The in vivo effect of Type I interferon (IFN) can be prolonged by administering the interferon in the form of a complex with an IFN binding chain of the human interferon &agr;/&bgr; receptor (IFNAR). Such a complex also improves the stability of the IFN and enhances the potency of the IFN. The complex may be a non-covalent complex or one in which the IFN and the IFNAR are bound by a covalent bond or a peptide. When bound by a peptide bond in the form of a fusion protein, the IFN may be separated from the IFNAR by means of a peptide linker. Such a fusion protein may be produced by recombinant DNA technology. Storing IFN in the form of such a complex improves the storage life of the IFN and permits storage under milder conditions than would otherwise be possible.