Abstract: Dimeric proteins having substantially the same biological activity as PDGF are disclosed. More specifically, the protein may have two substantially identical polypeptide chains, each of the chains being substantially homologous to the A-chain of PDGF. Alternatively, the protein may have two polypeptide chains that are substantially identical to the A-chain of PDGF. In addition, proteins comprising polypeptides that are variants or derivatives of the A-chain of PDGF are also disclosed. Therapeutic compositions containing these proteins and methods for enhancing the wound-healing process in warm-blooded animals are also disclosed.

Abstract: Dimeric proteins having substantially the same biological activity as PDGF are disclosed. More specifically, the proteins may have two polypeptide chains, one of the chains being a mosaic of amino acid sequences substantially identical to portions of the A- or B-chains of PDGF, the second of the chains being substantially homologous to either the A-chain or the B-chain of PDGF, the proteins being chemotactic or mitogenic for fibroblasts. Alternatively, each of the two polypeptide chains may be a mosaic of amino acid sequences as described above. Therapeutic compositions containing these proteins and methods for enhancing the wound-healing process in warm-blooded animals are also disclosed.

Abstract: Dimeric proteins having substantially the same biological activity as PDGF are disclosed. More specifically, the protein may have two substantially identical polypeptide chains, each of the chains being substantially homologous to the B-chain of PDGF. Alternatively, the protein may have two polypeptide chains that are substantially identical to the B-chain of PDGF. In addition, proteins comprising polypeptides that are variants or derivatives of the B-chain of PDGF are also disclosed. Therapeutic compositions containing these proteins and methods for enhancing the wound-healing process in warm-blooded animals are also disclosed.

Abstract: A method is provided for expressing human alpha-1-antitrypsin in yeast utilizing a wild-type strain and a hyperproduction mutant, GK100.

Abstract: Biologically active PDGF analogs expressed in eucaryotic cells are disclosed. The analogs are produced by yeast strains transformed with an extrachromosomal element composed of a strong transcriptional promoter directing the expression of a gene which encodes a protein having substantially the same biological activity as PDGF. Suitable genes include the v-sis gene or a derivative of the v-sis gene of simian sarcoma virus or portions thereof, or the human cDNA gene for PDGF or portions thereof. In particular, DNA sequences encoding polypeptides substantially homologous to the B chain of PDGF are preferred. A secretory signal sequence may be provided upstream of the gene, enabling secretion of the gene product from the host cell. Mitogenic activity is one of the biological activities possessed by these PDGF analogs, making them useful in promoting the growth of mammalian cells.

Abstract: Methods are disclosed for producing proteins having biological activity for blood coagulation mediated by Factor VIIa. The proteins are produced by mammalian host cells which have been stably transfected with a DNA construct containing a nucleotide sequence which codes at least partially for either Factor VII. The nucleotide sequence comprises a first nucleotide sequence encoding a calcium binding domain, joined to a second nucleotide sequence positioned downstream of the first sequence. In particular, the first nucleotide sequence may be derived from a genomic clone or cDNA clone of Factor VII. The second sequence encodes a catalytic domain for the serine protease activity of Factor VIIA. The joined sequences code for proteins having substantially the same biological activity for blood coagulation as Factor VIIa.

Abstract: Biologically active PDGF analogs expressed in yeast are disclosed. The analogs are produced by yeast strains transformed with an extrachromosomal element composed of a strong transcriptional promoter directing the expression of a gene which encodes a protein having substantially the same biological activity as PDGF. Suitable genes include the v-sis gene or a derivative of the v-sis gene of simian sarcoma virus or portions thereof, or the human cDNA gene for PDGF or portions thereof. A secretory signal sequence may be provided upstream of the gene, enabling secretion of the gene product from the yeast host cell. Mitogenic activity is one of the biological activities possessed by these PDGF analogs, making them useful in promoting the growth of mammalian cells.

Abstract: Methods for expressing a variety of biologically active PDGF analogs in eucaryotic cells are disclosed. The methods generally comprise introducing into a eucaryotic host cell a DNA construct capable of directing the expression and secretion of biologically active PDGF analogs in eucaryotic cells. The DNA construct contains a transcriptional promoter followed downstream by a suitable DNA sequence. The DNA sequence may encode a protein substantially homologous to the A-chain or the B-chain of PDGF, or a portion thereof, or an A-B heterodimer. In addition, a portion of the DNA sequence may encode at least a portion of the A-chain, while another portion encodes at least a portion of the B-chain of PDGF. Eucaryotic cells transformed with these DNA constructs are also disclosed. Methods of promoting the growth of mammalian cells, comprising incubating the cells with a biologically active PDGF analog expressed by a eucaryotic host cell transformed with such a DNA construct, are also disclosed.

Abstract: Methods are provided for producing sites specific mutagenized alpha-1-antitrypsin. Particular mutants are formed having a mutation in the active site of alpha-1-antitrypsin at amino acid position 358 and at amino acid position 342.