Abstract: Novel proinsulins and glargine, aspart and Lis-Pro proinsulin analogs having specific amino acid and/or nucleic acid modifications suitable for improved methods of insulin production, as well as novel and highly efficient processes for preparing the same. The novel proinsulins and proinsulin analogs may be converted into human insulin and insulin analogs, respectively, that are useful in therapeutic preparations.

Abstract: Novel proinsulins and glargine, aspart and Lis-Pro proinsulin analogs having specific amino acid and/or nucleic acid modifications suitable for improved methods of insulin production, as well as novel and highly efficient processes for preparing the same. The novel proinsulins and proinsulin analogs may be converted into human insulin and insulin analogs, respectively, that are useful in therapeutic preparations.

Abstract: Lis-Pro modified proinsulin sequences that have a modified C-peptide amino acid and/or nucleic acid modification are presented. Methods for producing Lis-Pro insulin analogs are also disclosed. Highly efficient processes for preparing the Lis-Pro insulin analogs and improved preparations containing the Lis-Pro insulin analogs prepared according to the methods described herein are also provided.

Abstract: Disclosed herein are novel and improved preparations and methods for manufacturing substantially liquid preparations of recombinant human insulin API. The purified recombinant human insulin Active Pharamaceutical Ingredient (API) preparations are substantially free of by-products associated with the lyophilization and/or crystallization. The methods for manufacturing the substantially liquid recombinant human insulin API preparations are provided with optional steps for subjecting the recombinant insulin preparation to lyophilization and/or crystallization. Enhanced yield of recombinant insulin of greater purity are thereby provided according to the present invention. Highly purified formulations of recombinant human insulin of the API insulin preparations disclosed herein are also provided. Stably transformed E.

Abstract: Aspart modified proinsulin sequences that have a modified C-peptide amino acid and/or nucleic acid modification for producing aspart insulin analogs are provided. Highly efficient processes for preparing the aspart insulin analogs and improved preparations containing the aspart insulin analogs prepared according to the methods described herein are also provided.

Abstract: Aspart modified proinsulin sequences that have a modified C-peptide amino acid and/or nucleic acid modification for producing aspart insulin analogs are provided. Highly efficient processes for preparing the aspart insulin analogs and improved preparations containing the aspart insulin analogs prepared according to the methods described herein are also provided.

Abstract: Glargine proinsulin sconstructs that have a modified C-peptide amino acid and/or nucleic acid sequence for producing glargine insulin analogs are provided. Highly efficient processes for preparing the glargine insulin analogs and improved preparations containing the glargine insulin analogs prepared according to the methods described herein are also provided.

Abstract: Lis-Pro modified proinsulin sequences that have a modified C-peptide amino acid and/or nucleic acid modification are presented. Methods for producing Lis-Pro insulin analogs are also disclosed. Highly efficient processes for preparing the Lis-Pro insulin analogs and improved preparations containing the Lis-Pro insulin analogs prepared according to the methods described herein are also provided.

Abstract: Disclosed herein are novel and improved preparations and methods for manufacturing substantially liquid preparations of recombinant human insulin API. The purified recombinant human insulin Active Pharmaceutical Ingredient (API) preparations are substantially free of by-products associated with the lyophilization and/or crystallization. The methods for manufacturing the substantially liquid recombinant human insulin API preparations are provided with optional steps for subjecting the recombinant insulin preparation to lyophilization and/or crystallization. Enhanced yield of recombinant insulin of greater purity are thereby provided according to the present invention. Highly purified formulations of recombinant human insulin of the API insulin preparations disclosed herein are also provided. Stably transformed E. coli cell banks (WCB) capable of expressing the recombinant human insulin are also provided.

Abstract: Novel pro-insulin having specific amino acid and/or nucleic acid modifications suitable for improved methods of insulin production are provided. Novel and highly efficient processes for preparing the pro-insulin preparations and preparations containing them are also disclosed. The novel pro-insulin preparations may be converted into human insulin useful in therapeutic preparations. Novel peptides of the C-peptide, and N terminus, including RREAEALQVGQVELGGGPGAGSLQPLALEGSLQAR (SEQ ID NO: 32), and MHHHHHHGGR (SEQ ID NO: 2) respectively are provided, as well as the unique nucleic acid molecules encoding them.

Abstract: Novel pro-insulin having specific amino acid and/or nucleic acid modifications suitable for improved methods of insulin production are provided. Novel and highly efficient processes for preparing the pro-insulin preparations and preparations containing them are also disclosed. The novel pro-insulin preparations may be converted into human insulin useful in therapeutic preparations. Novel peptides of the C-peptide, and N terminus, including RREAEALQVGQVELGGGPGAGSLQPLALEGSLQAR (SEQ ID NO:32), and MHHHHHHGGR (SEQ ID NO:36) respectively are provided, as well as the unique nucleic acid molecules encoding them.

Abstract: Novel pro-insulin having specific amino acid and/or nucleic acid modifications suitable for improved methods of insulin production are provided. Novel and highly efficient processes for preparing the pro-insulin preparations and preparations containing them are also disclosed. The novel pro-insulin preparations may be converted into human insulin useful in therapeutic preparations. Novel peptides of the C-peptide, and N terminus, including RREAEALQVGQVELGGGPGAGSLQPLALEGSLQAR (SEQ ID NO: 32), and MHHHHHHGGR (SEQ ID NO: 2) respectively are provided, as well as the unique nucleic acid molecules encoding them.

Abstract: The present invention provides adducts of human t-PA derivatives, which comprise a t-PA derivative that lacks the Finger, Growth Factor and Kringle 1 domains, bound to an amphipathic molecule. The invention also provides methods for preparing the adducts and compositions for the treatment of thromboembolic disorders.

Abstract: Long chain alkyl and alkenyl sulfonates, sulfates and sulfoalkyl alkanoate salts, administered intravaginally for contraception.

Abstract: A contraceptive device for intravaginal use comprising a bioinsoluble, biocompatible polyurethane and an acrosin inhibitor.

Abstract: Introduction of a pharmaceutically acceptable non-toxic cation salt of a straight-chain or branched chain alkyl sulfonate having from 11 to 16 carbon atoms into the uterine lumen or vaginal cavity prevents conception. Sodium tetradecyl sulfonate is preferred.

Abstract: Introduction of a pharmaceutically acceptable non-toxic cation salt of a sulfoalkyl alkanoate, for example, sodium sulfopropyl dodecanoate, into the uterine lumen or vaginal cavity prevents conception.

Abstract: Introduction of a compound of the formula:R--OSO.sub.3 --Mwherein R is:(a) C.sub.11 -C.sub.30 straight chain alkyl or alkenyl;(b) C.sub.10 -C.sub.30 branched chain alkyl or alkenyl, the .alpha.-carbon of which is not branched; or(c) C.sub.13 -C.sub.30 branched chain alkyl or alkenyl, the .alpha.-carbon of which is branched,and M is a pharmaceutically acceptable non-toxic cation; into the uterine lumen or vaginal cavity prevents conception. Sodium n-tetradecyl sulfate is preferred.

Abstract: Introduction of a pharmaceutically acceptable non-toxic cation salt of a sterol sulfate into the uterine lumen or vaginal cavity prevents conception. Potassium or pyridinium .beta.-sitosteryl sulfate is preferred.