Abstract: A nucleic acid encodes a novel fusion protein. The fusion protein contains a cysteinized variant of an RNase disclosed in U.S. Pat. No. 6,239,257 B1.

Abstract: A nucleic acid encodes a novel RNase. The RNase has an amino acid sequence in which an amino acid sequence disclosed in United States Patent U.S. Pat. No. 6,239,257 B1 is preceded by a different N-terminal residue or leader sequence.

Abstract: A cysteinized variant of an RNase disclosed in U.S. Pat. No. 6,239,257 B1 is disclosed. A targeting moiety can be conjugated to the cysteine residue.

Abstract: A cysteinized variant of an RNase disclosed in U.S. Pat. No. 6,239,257 B1 is disclosed. A targeting moiety can be conjugated to the cysteine residue.

Abstract: A fusion protein contains a cysteinized variant of an RNase disclosed in U.S. Pat. No. 6,239,257 B1.

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: 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: The present invention relates to a method of inhibiting protein synthesis comprising contacting 28S rRNA of a protein synthesizing system with a protein synthesis inhibitory amount of an oligonucleotide that hybridizes to the -sarcin recognition domain loop of said 28S rRNA under condition such that hybridization occurs. The invention also relates to oligonucleotides suitable for use in such a method.