Abstract: A process for purifying an antibody is provided. In this process, a mixture containing the antibody and a contaminant is subjected to low pH hydrophobic interaction chromatography (LPHIC) at low salt concentration. The antibody is eluted from the column in the fraction which does not bind thereto. This process can be preceded and followed by other purification steps.

Abstract: A process for purifying an antibody is provided. In this process, a mixture containing the antibody and a contaminant is subjected to low pH hydrophobic interaction chromatography (LPHIC) at low salt concentration. The antibody is eluted from the column in the fraction which does not bind thereto. This process can be preceded and followed by other purification steps.

Abstract: The present invention relates to novel, stable recombinant gamma interferons exhibiting in greater or less degree the antiviral and antiproliferative activity in humans and pH 2 labile properties characteristic of native human gamma interferon. The amino acid sequence of such an interferon comprises, from the N-terminus: X-Y-Asp . . . Thr   1   2       126 wherein X is a methionine residue or hydrogen and Y is a glutamine residue, or, where X is hydrogen, Y is either a glutamine or a pyroglutamate residue.

Abstract: A process for purifying an antibody is provided. In this process, a mixture containing the antibody and a contaminant is subjected to low pH hydrophobic interaction chromatography (LPHIC) at low salt concentration. The antibody is eluted from the column in the fraction which does not bind thereto. This process can be preceded and followed by other purification steps.

Abstract: The present invention relates to novel, stable recombinant gamma interferons exhibiting in greater or less degree the antiviral and antiproliferative activity in humans and pH 2 labile properties characteristic of native human gamma interferon. The amino acid sequence of such an interferon comprises, from the N-terminus: ##STR1## wherein X is a methionine residue or hydrogen and Y is a glutamine residue or, where X is hydrogen, Y is either a glutamine or a pyroglutamate residue.

Abstract: A process for purifying an antibody is provided. In this process, a mixture containing the antibody and contaminant is subjected to low pH hydrophobic interaction chromatography (LPHIC) optionally at low salt concentration. The antibody is eluted from the column in the fraction which does not bind thereto. This process can be preceded and followed by other purification steps.

Abstract: Provided are methods for the production of mixtures of interferon (IFN)-.gamma. polypeptides. The methods employ a single species of IFN-.sub..gamma. DNA having codons for Met-Gln and for residues 2-143 of the mature human IFN-.sub..gamma. amino acid sequence. Expression of such DNA in a suitable recombinant host cell affords a mixture of polypeptides having N-terminal Met-Gln, H-Gln, or H-pyroglutamate residues and C-termini at Arg.sup.139, Ser.sup.142, or Gln.sup.143 of the mature IFN-.sub..gamma. sequence. The polypeptides so produced exhibit the antiviral and antiproliferative activities as well as the acid lability characteristic of native human IFN-.sub..gamma..

Abstract: The present invention relates to novel, stable recombinant gamma interferons exhibiting in greater or less degree the antiviral and antiproliferative activity in humans and pH 2 labile properties characteristic of native human gamma interferon. The amino acid sequence of such an interferon comprises, from the N terminus: ##STR1## wherein X is a methionine residue or hydrogen and Y is a glutamine residue or, where X is hydrogen, Y is either a glutamine or a pyroglutamate residue.

Abstract: The present invention relates to novel, stable recombinant gamma interferons exhibiting in greater or less degree the antiviral and antiproliferative activity in humans and pH 2 labile properties characteristic of native human gamma interferon. The amino acid sequence of such an interferon comprises, from the N terminus: ##STR1## wherein X is a methionine residue or hydrogen and Y is a glutamine residue or, where X is hydrogen, Y is either a glutamine or a pyroglutamate residue.