Abstract: New uses of proteoglycans to bind and present growth factors, methods of accelerating wound, tissue or bone repair using such proteoglycans, pharmaceutical compositions of such proteoglycans, and scaffolds coated with such proteoglycans are disclosed. The proteoglycan of the invention is derived from domain I or perlecan.

Abstract: New uses of proteoglycans to bind and present growth factors, methods of accelerating wound, tissue or bone repair using such proteoglycans, pharmaceutical compositions of such proteoglycans, and scaffolds coated with such proteoglycans are disclosed. The proteoglycan of the invention is derived from domain I or perlecan.

Abstract: Monoclonal antibodies for selective immunological determination of high molecular weight, intact laminin forms in body fluids. The present invention relates to monoclonal antibodies for the selective immunological determination of high molecular weight forms of laminin in body fluids, to a process for preparing these antibodies, and to their use for diagnosing diseases. The antibodies according to the invention preferably bind to intact, native laminin, in particular to the structures of the laminin P1 domain of the laminin which are folded in a native manner.

Abstract: Monoclonal antibodies directed to the laminin P1 domain for selective immunological determination of native, high molecular weight, intact laminins in body fluids; a process for preparing these antibodies; and their use for diagnosing diseases. These antibodies preferably bind to intact, native laminin, in particular to the structures of the laminin P1 domain of laminin which are folded in a native manner.

Abstract: It is possible with the aid of a monoclonal antibody which is specifically directed against an epitope of amino-terminal procollagen peptide (type III) which is not present on the fragment Col 1, and of a second monoclonal or polyclonal antibody against an epitope of amino-terminal procollagen peptide (type III), to determine said peptide with great accuracy. It is also, possible, with the aid of a monoclonal antibody which is specifically directed against an epitope of amino-terminal procollagen peptide (type III) which is not present in Col 1, to determine with great accuracy said procollagen peptide in body fluids.

Abstract: High affinity binding of nidogen to laminin is mediated by an EGF-like repeat .gamma.1III4 of the mouse laminin .gamma.1 chain and has now been restricted to two short non-contiguous regions of its 56 residue sequence by use of synthetic peptides and recombinant mutants. Disulfide loop a,b of the repeat and a modified loop a,c could completely inhibit binding, with a 5,000-fold or 300-fold reduced affinity, respectively. Synthetic loops c and d lacked inhibitory activity. Some binding contribution of Try819 in loop c was, however, shown by mutation and side chain modification. Together with studies of loop chimeras, this indicated a distinct cooperativity between the two binding sites. The major binding site of loop a was localized to the heptapeptide NIDPNAV (position 798-804). A change of Asp800 to Asn or Ala803 to Val caused a strong reduction in binding activity, while only small effects were observed for the changes Pro801 to Gln and Ile799 to Val.

Abstract: The invention relates to a method for the immunological determination of basal membrane low-density heparan sulfate-proteoglycan in body fluids, and to the preparation or obtaining of a low-density heparan sulfate-proteoglycan suitable for this purpose, and of the corresponding highly specific antibodies.

Abstract: Basement membrane proteins are isolated as functioning proteins in relatively large amounts from human or animal tissues in aqueous solution in the presence of a chelating agent. It is possible to use these proteins to obtain highly specific antibodies which are used for the immunological determination of these proteins.

Abstract: The present invention provides human characterized by a molecular weight of about 170,000 Dalton, a hexameric structure with monomeric subunits with a molecular weight of about 28,000 Dalton and a carbohydrate content of about 2%.The present invention provides a process for obtaining and purifying globular domain NC1 of basal membrane collagen, wherein human or animal tissue is subjected to a first limiting treatment with bacterial collagenase, the degradation products obtained are separated from non-collagen proteins by chromatography on a weakly basic anion exchanger, the collagen degradation products are then subjected to a second collagenase digestion at an elevated temperature and the globular domain NC1 is purified by molecular sieve fractionation.Furthermore, the present invention is concerned with the use of this for the determination in body fluids in the case of the use of their antibodies, as well as far the detection of antibodies directed thereagainst in body fluids.

Abstract: The present invention provides a process for the immunological determinat of proteins in body fluids which display a non-parallel inhibition curve to a reference inhibitor, wherein specific monovalent antibody fragments are used as antiserum.

Abstract: The antigens procollagen peptide (type (III) and procollagen peptide col 1 (type III) can be determined together immunologically by either(a) reacting a specified amount in each case of labeled procollagen peptide (type III) or procollagen peptide col 1 (type III) and a highly specific antiserum containing antibodies having affinity for both the antigens mentioned together with a sample having an unknown content of procollagen peptide (type III) and/or procollagen peptide col 1 (type III), separating off the antigen-antibody complex formed and measuring the amount of labeling in the complex and/or in the supernatant, or(b) bringing a specified amount of the highly specific antiserum to reaction with a sample having an unknown content of procollagen peptide (type III) and/or procollagen peptide col 1 (type III), fixing the unreacted amount of the antibody to procollagen peptide (type III) or procollagen peptide col 1 (type III) bound to a support, and bringing to reaction with a labeled second antibody, and th

Abstract: This invention relates to a process for the immunological determination of asal membrane material in body fluids and provides new basal membrane fragments suitable for such determination, and a process for their preparation.

Abstract: For the radioimmunological determination of procollagen (type III) and procollagen peptide (type III) a certain amount of radioactively tagged procollagen (type III) or procollagen peptide (type III) and a highly specific anti-procollagen (type III) serum or anti-procollagen peptide (type III) serum are brought to reaction together with a sample of an unknown content of procollagen (type III) or procollagen peptide (type III), the formed antigen-antibody complex is separated, desirably by the addition of a second antibody against the highly specific antiserum, and the radioactivity of the complex or of the supernatant liquid is measured. Highly purified procollagen peptide (type III) suitable for this purpose is obtained by the degradation of tissue or body fluids with collagenase and purification by immune adsorption and chromatography.