Eli Lilly and Company

Gerald W Becker

John Edward Hale

Warren C MacKellar

Thomas C Furman

James P McDonough

Derrick Ryan Witcher

Radmila Micanovic

Radhakrishnan Rathnachalam

Sheng-Hung Rainbow Tschang

Carl J Shaar

Timothy Wayne Noblitt

Fredric Jay Cohen

Ralph M Riggin

Victor John Wroblewski

Patricia Ann Gonzalez-DeWhitt

Christy Michelle Newton

Disclosed are polypeptide analogs of FLINT, polydeoxynucleotides encoding FLINT analogs, and methods of using FLINT analogs and polydeoxynucleotides. The FLINT analogs of the invention include polypeptides having the amino acid sequence of FLINT, modified at one or more positions with amino acid substitutions, and include fragments thereof, as well as Fc fusions comprising FLINT and FLINT analogs.

Flint polypeptide analogs

A leptin binding protein, inter-alpha-trypsin inhibitor heavy chain related protein (IHRP), specifically binds leptin, the obesity gene product. The specific leptin binding proteins enable modulation of free leptin levels, immobilization and assay of bound/free leptin.

Leptin bound to inter-alphatrypsin inhibitor and uses thereof

The present invention provides anti-obesity proteins, which when administered to a patient regulate fat tissue. Accordingly, such agents allow patients to overcome their obesity handicap and live normal lives with much reduced risk for type II diabetes, cardiovascular disease and cancer.

Anti-obesity proteins

This disclosure relates to new compounds and to a process for the controlled conversion of such compounds to produce a Protein that comprises an amino acid sequence which is useful as a precursor to human insulin or to a modified human insulin, the amino terminus portion of which sequence does not define a cathepsin C dipeptide removal stop point. The compounds have the formula Met-Y-Protein in which Y is Tyr or Arg.

Enzymatic removal of a protein amino-terminal sequence

This specification describes modified growth hormone having substantially diminished insulin-like and diabetogenic potencies relative to the native hormone with retention of substantially all of the anabolic potency of the native hormone. The modified growth hormone has the following structure: (a) elimination of from 1-5 to 1-19 amino acid residues from the amino terminus of the hormone; (b) cleavage of a peptide bond at any point from the carboxy moiety of residue 127 to residue 153; and (c) optionally, elimination of one or more of amino acid residues 128-152 of the hormone.

Proteins having growth hormone anabolic properties with reduced effect

A sulfoxide of human growth hormone has been produced and characterized. The sulfoxide derivative arises from a selective oxidation of Met.sup.14. The sulfoxide exhibits full biological activity.

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Indianapolis, IN, United States of America

Gerald W Becker