Other

Scios Nova, Inc.

California Biotechnology Inc.

Scios Inc.

Douglas I Buckley

Bradley J Benson

Robert M Scarborough

James W Schilling, Jr

Robert T White

David D Lesikar

Kate B Silverness

Asha Naidu

Joel F Habener

Ziyang Zhong

Janakiraman Ramachandran

Taymar E Hartman

Donald H Yamashiro

N Stephen Pollitt

Svetlana Mojsov

Joanne B Mallory

James R Hagman

Peter A Stathis

Improvements in methods for manufacturing glow in-the-dark targets are disclosed. This provides an ink that produces images that will glow in the dark for an extended period of time after the ink has been exposed to natural or artificial light. This can be used for flexographic printing, offset printing, gravure printing, and screen printing applications. The ink includes a phosphorescent pigment and optionally includes a colorant on a substrate of paper, plastic or metal. The phosphorescent pigment material is not coated prior to mixing with other ink components. The pigment material has a particle diameter size of about 600 mesh to about 1500 mesh. The ink includes a colorant (optional), a thermoplastic resin binder, a charge-controlling agent, a release agent, as well as the phosphorescent pigment.

Methods for manufacturing glow in-the-dark targets

A method is described for producing a peptide having a pI above 8 or below 5 wherein the peptide is expressed as a fusion protein in which it is linked to a fusion partner through an acid cleavage site. The peptide is released from the fusion partner by acid cleavage in the absence of chaotrope. The fusion partner and its acid cleavage products, if any, have a net charge sufficiently different from that of the desired peptide to allow isolation of the peptide by ion-exchange chromatography.

Method for producing a peptide with a pI above 8 or below 5

The invention provides effective analogs of the active GLP-1 peptides, 7-34, 7-35, 7-36, and 7-37, which have improved characteristics for treatment of diabetes Type II. These analogs have amino acid substitutions at positions 7-10 and/or are truncated at the C-terminus and/or contain various other amino acid substitutions in the basic peptide. The analogs may either have an enhanced capacity to stimulate insulin production as compared to glucagon or may exhibit enhanced stability in plasma as compared to GLP-1 (7-37) or both. Either of these properties will enhance the potency of the analog as a therapeutic. Analogs having D-amino acid substitutions in the 7 and 8 positions and/or N-alkylated or N-acylated amino acids in the 7 position are particularly resistant to degradation in vivo.

GLP-1 analogs useful for diabetes treatment

Methods are provided for the isolation and purification of recombinant lung surfactant protein. The methods involve a multistep procedure including extraction with a C.sub.1 -C.sub.4 aliphatic alcohol and chromatographic purification steps which employ a C.sub.1 -C.sub.4 aliphatic alcohol as eluant. Purified proteins obtained using the disclosed isolation and purification steps are provided as well.

Isolation and purification of lung surfactant protein

Various specific human SP-18 and human SP-5 derived peptides have alveolar surfactant protein (ASP) activity. These peptides are prepared using synthetic methods or by recombinant techniques.

DNA encoding analogs of human alveolar surfactant protein SP-5

DNA encoding and expression systems for alveolar surfactant proteins

Various specific human SP-18 and human SP-5 derived peptides have alveolar surfactant protein (ASP) activity. These peptides are prepared using synthetic methods or by recombinant techniques. The peptides of the invention include surfactant proteins having serine replacements for the cysteines.

Alveolar surfactant proteins having cys to ser mutations

A fully steroidogenically active analog of ACTH is disclosed. The analog differs from natural ACTH in that phenylalanine replaces tyrosine in the second position on the peptide chain; and norleucine replaces methionine in the fourth position on the peptide chain. The analog may be iodinated to yield [I]Tyr.sup.2 -Phe.sup.2,Nle.sup.4 -ACTH, which also retains full steroidogenic activity. When labeled with iodine-125 the analog is useful in following steroidogenic processes and also in radioimmunoassays for ACTH.

Biologically active analogs of ACTH and radioimmuno assay therefor

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Woodside, CA, United States of America

Douglas I Buckley