proteinase/neoplasms

REFERENCE TO SEQUENCE LISTINGS, A TABLE, OR A COMPUTER PROGRAM LISTING COMPACT DISC APPENDIX Not Applicable BACKGROUND OF THE INVENTION Cancers are collectively a very large group of devastating diseases characterized by uncontrolled cell division, growth, invasiveness and the capability of

STATEMENT REGARDING FEDERALLY SPONSORED RESEARCH OR DEVELOPMENT This invention was not sponsored by any federal research or development fund. BACKGROUND OF THE INVENTION The idea of using proteinases to do solid-tumor microsurgery has led to the discovery of a new class of drugs that can eliminate

CROSS REFERENCE TO RELATED APPLICATIONS This application is a 35 U.S.C. .sctn.371 National Phase Entry Application from PCT/DE01/01510, filed Apr. 18, 2001 and designating the United States. This application further claims foreign priority to German application DE 100 20 125.3, filed Apr. 18,

FIELD OF THE INVENTION This invention relates to selective peptidyl inhibitors of cancer procoagulant (CP), a protein elaborated by malignant, but not normal, animal and human cells, and to the use of these selective peptidyl inhibitors in cancer therapy and in CP removal from blood. BACKGROUND OF

BACKGROUND OF THE INVENTION Cysteine proteinases containing a highly reactive cysteine residue with a free thiol group at the active site have been known as playing an important role in certain conditions distinguished by aberrant protein turnover such as: muscular dystrophy (Am. J. Pathol. 1986,

BACKGROUND OF INVENTION Cysteine proteinases containing a highly reactive cysteine residue with a free thiol group at the active site have been known as playing important role in certain conditions distinguished by aberrant protein turnover such as: muscular dystrophy (Am. J. Pathol. 1986, 122,

BACKGROUND OF THE INVENTION Cysteine proteinases containing a highly reactive cysteine residue with a free thiol group at the active site have been known as playing an important role in certain conditions distinguished by aberrant protein turnover such as: muscular dystrophy (Am. J. Pathol. 1986,

BACKGROUND OF THE INVENTION Cysteine proteinases containing a highly reactive cysteine residue with a free thiol group at the active site have been known as playing an important role in certain conditions distinguished by aberrant protein turnover such as: muscular dystrophy (Am. J. Pathol. 1986,

BACKGROUND OF THE INVENTION The prostate specific antigen (PSA) was first purified from prostatic tissue (Wang et al. Invest Urol 1979), but the same protein was almost simultaneously and independently characterized in the seminal plasma (Hara et al. J Lab Clin Med 1989; Graves et al. N Engl J Med

FIELD OF THE INVENTION The present invention related generally to novel molecules and more particularly novel proteinaceous molecules involved in or associated with regulation of cell activities and/or viability. The present invention is particularly directed to novel serene proteinases and a novel

STATEMENT REGARDING SEQUENCE LISTING The Sequence Listing associated with this application is provided in text format in lieu of a paper copy, and is hereby incorporated by reference into the specification. The name of the text file containing the Sequence Listing is

FIELD OF THE INVENTION The invention relates to an enzyme, arginine deiminase. In particular, it relates to a unique arginine deiminase isolated from mycoplasmas. More particularly, the invention is directed to a mycoplasmal proteinase K resistant arginine deiminase and to a method of preparing

BACKGROUND TO THE INVENTION Proteinases form a substantial group of biological molecules which to date constitute approximately 2% of all the gene products identified following analysis of several completed genome sequencing programmes. Proteinases have evolved to participate in an enormous range of

SEQUENCE LISTING The instant application contains a Sequence Listing which has been submitted in ASCII format via EFS-Web and is hereby incorporated by reference in its entirety. Said ASCII copy, created on Feb. 15, 2012, is named 86519CON.txt and is 11,216 bytes in size. BACKGROUND OF THE

BACKGROUND OF THE INVENTION Full length active .alpha..sub.1 proteinase inhibitor (.alpha..sub.1PI, .alpha..sub.1 antitripsin) is composed of 394 amino acids (aa) having a mass of approximately 55 kDa when fully glycosylated (Berninger, 1985). Hepatocytes are the primary source of .alpha..sub.1PI,