Abstract: Two follistatin proteins with inhibin-like activity were isolated from porcine follicular fluid using heparin-Sepharose affinity chromatography, followed by gel filtration on Sephacryl S-200 and then six steps of high-performance liquid chromatography. The larger protein has 315 residues and is believed to be glycosylated. The smaller protein is a 288-residue, C-terminally shortened version thereof. These proteins specifically inhibit basal secretion of FSH, but not of LH, in a rat anterior pituitary monolayer culture system. The half-maximal effective dose for both is 2.5-6.0 ng/ml. Human and rat follistatins exhibit very high homology with the porcine protein, with the human differing from porcine in only 4 residues out of 315 and with the rat differing from porcine in only 8 residues out of 315. Using the porcine amino acid sequence information, cDNA clones encoding these proteins were identified from a porcine ovarian cDNA library.

Abstract: A DNA construct is provided comprising DNA encoding a mature BMP-2 upstream of which is DNA encoding a precursor portion of a mammalian protein other than the BMP-2. Also provided are mammalian expression vectors and hosts containing such a DNA construct and methods for improved expression using such construct.

Abstract: Tissue plasminogen activator analogs exhibiting greater specificity for fibrin than native t-PA are disclosed. The analogs include the K1 domain of native t-PA replaced with another kringle domain mediating the binding of the analog to fibrin. The kringle contains six cysteine residues. The t-PA analogs may further include a variety of substitutions and modifications. Pharmaceutical compositions containing one or more of the t-PA analogs along with a physiologically acceptable carrier or diluent are also disclosed.

Abstract: Biologically active mutant tissue plasminogen activators are disclosed wherein site directed mutagenesis, for example, of a two-chain activation site renders the mutants resistant to conversion to the two-chain form.

Abstract: DNA sequences are provided which encode a form of basic fibroblast growth factor lacking one of the alanine residues immediately following the N-terminal methionine residue of the primary translation product. The DNA sequences can be expressed to produce basic fibroblast growth factor having a homogeneous N-terminus.