Abstract: Methods for recombinantly producing new RNases, as well as previously-known RNases, are disclosed. The new RNases are active against human carcinoma cells.

Abstract: Methods for recombinantly producing new RNases, as well as previously-known RNases, are disclosed. The new RNases are active against human carcinoma cells.

Abstract: Methods for recombinantly producing new RNases, as well as previously-known RNases, are disclosed. The new RNases are active against human carcinoma cells.

Abstract: Methods for recombinantly producing new RNases, as well as previously-known RNases, are disclosed. The new RNases are active against human carcinoma cells.

Abstract: Methods for recombinantly producing new RNases, as well as previously-known RNases, are disclosed. The new RNases are actable against human carcinoma cells.

Abstract: Methods for recombinantly producing new RNases, as well as previously-known RNases, are disclosed. The new RNases are active against human carcinoma cells.

Abstract: Methods for recombinantly producing new RNases, as well as previously-known RNases, are disclosed. The new RNases are active against human carcinoma cells.

Abstract: Ribonuclease DNA coding for an amino acid sequence beginning with a residue of glutamine is introduced into a vector of pET22b(+) plasmid to form recombinant plasmid DNA that begins with a Pel B leader sequence. The recombinant plasmid DNA is used to transform an E.coli BL21(DE3) host. Signal peptidase enzyme present in the host cell cleaves the pelB leader sequence during signal processing and thereby allows the glutamine residue to autocyclize to pyroglutamic acid. In this way, the Ribonuclease can be produced directly, i.e. without a separate step of cleaving the initial N-terminal methionine residue.

Abstract: pET11d-rOnc(Q1, M23L) DNA is subjected to two different site-directed mutations, each using an overlapping PCR protocol. One of the site-directed mutations changes the amino acid residue at position 23 of the encoded protein from leucine to methionine, whereby the encoded protein can be made into ranpirnase by cleaving the N-terminal methionine residue and allowing the adjacent glutamine residue to autocyclize. The other site-directed mutation changes the amino acid residue at position 72 of the encoded protein from serine to cysteine, thereby producing an encoded protein that can be made into a cysteinized ranpirnase by cleaving the N-terminal methionine residue and allowing the adjacent glutamine residue to autocyclize.

Abstract: A first substance (such as the peptide aldehydes LLnL and LVP) inhibits the function of intracellular proteasome. A second substance (such as ranpirnase) inhibits intracellular protein synthesis or increases intracellular expression of a cyclin-dependent kinase (CDK) inhibitor. Both substances are administered in such a manner that the effects thereof are coincident. The cell cycle of affected tumor cells is therefore arrested and the cells die of apoptosis.

Abstract: A protein family includes four proteins that are bioactive against human tumor cell lines. The proteins are derived from eggs of the Rana pipiens frog, and are members of the superfamily of pancreatic ribonucleases.

Abstract: pET11d-rOnc(Q1, M23L) DNA is subjected to two different site-directed mutations, each using an overlapping PCR protocol. One of the site-directed mutations changes the amino acid residue at position 23 of the encoded protein from leucine to methionine, whereby the encoded protein can be made into ranpirnase by cleaving the N-terminal methionine residue and allowing the adjacent glutamine residue to autocyclize. The other site-directed mutation changes the amino acid residue at position 72 of the encoded protein from serine to cysteine, thereby producing an encoded protein that can be made into a cysteinized ranpirnase by cleaving the N-terminal methionine residue and allowing the adjacent glutamine residue to autocyclize.

Abstract: A pharmaceutical known by the trademark ONCONASE, as described in pending commonly owned application application number 07/436,141 filed Nov. 13, 1989, is combined with two forms of another drug known as Lovastatin. The combination of ONCONASE with Lovastatin has unexpected bioactivity in vitro against ASPC-1 human pancreatic adenocarcinoma cells, A-549 human lung carcinoma cells and HT-520 human squamous cell lung carcinoma cells.

Abstract: Rana pipiens eggs are subjected to fertilization and the embryos are grown to a predetermined stage of development. The embryos and unfertilized eggs are then subjected to mechanical processing in the presence of a weakly acidic buffer to produce an extract. The extract is subjected to ion-exchange chromatography and size-exclusion chromatography.The resulting pharmaceutical has activity against certain cancer cells. The amino acid sequence and composition of the pharmaceutical are disclosed.

Abstract: A pharmaceutical to be sold under the ONCONASE trademark, as described in pending commonly owned application application Ser. No. 07/436,141 filed Nov. 13, 1989 is combined with other drugs sold under the trademarks TAMOXIFEN and STELAZINE. The combination of ONCONASE with TAMOXIFEN has unexpected bioactivity in vitro against ASPC-1 human pancreatic adenocarcinoma cells and the combination of ONCONASE with STELAZINE has unexpected bioactivity in vitro against A-549 human lung carcinoma cells.

Abstract: A pharmaceutical known by the trademark ONCONASE, as described in pending commonly owned application application Ser. No. 07/436,141 filed Nov. 13, 1989, is combined with drugs sold under the names cisplatin, Melphalan and Doxorubicin HCl. The combinations of ONCONASE with these drugs has unexpected bioactivity in vitro against OVCAR-3 human ovarian adenocarcinoma cells.

Abstract: Rana pipiens eggs are subjected to fertilization and the embryos are grown to a predetermined stage of development. The embryos and unfertilized eggs are then subjected to mechanical processing in the presence of a weakly acidic buffer to produce an extract. The extract is subjected to ion-exchange chromatography and size-exclusion chromatography.The resulting pharmaceutical has activity against certain cancer cells. A partial amino acid sequence of the pharmaceutical is disclosed.