Patents by Inventor Roger C. L. Guillemin
Roger C. L. Guillemin has filed for patents to protect the following inventions. This listing includes patent applications that are pending as well as patents that have already been granted by the United States Patent and Trademark Office (USPTO).
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Patent number: 5182375Abstract: Two follistatin proteins with inhibin-like activity were isolated from porcine follicular fluid using heparin-Sepharose affinity chromatography, followed by gel filtration on Sephacryl S-200 and then six steps of high-performance liquid chromatography. The larger protein has 315 residues and is believed to be glycosylated. The smaller protein is a 288-residue, C-terminally shortened version thereof. These proteins specifically inhibit basal secretion of FSH, but not of LH, in a rat anterior pituitary monolayer culture system. The half-maximal effective dose for both is 2.5-6.0 ng/ml. Human and rat follistatins exhibit very high homology with the porcine protein, with the human differing from porcine in only 4 residues out of 315 and with the rat differing from porcine in only 8 residues out of 315. Using the porcine amino acid sequence information, cDNA clones encoding these proteins were identified from a porcine ovarian cDNA library.Type: GrantFiled: May 31, 1991Date of Patent: January 26, 1993Assignee: The Salk Institute for Biological StudiesInventors: Nicholas C. K. Ling, Naoto Ueno, Shunichi Shimasaki, Frederick S. Esch, Shao-Yao Ying, Roger C. L. Guillemin
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Patent number: 5041538Abstract: Two follistatin proteins with inhibin-like activity were isolated from porcine follicular fluid using heparin-Sepharose affinity chromatography, followed by gel filtration on Sephacryl S-200 and then six steps of high-performance liquid chromatography. Each isolated molecule is a monomer having a molecular weight of at least about 32,000 daltons. Microsequencing revealed the NH.sub.2 -terminal portions both to be Gly-Asn-Cys-Trp-Leu-Arg-Gln-Ala-Lys-Asn-Gly-Arg-Cys-Gln-Val-Leu. The larger protein has 315 residues and is believed to be glycosylated. The smaller protein is a 288-residue, C-terminally shortened version thereof. These proteins specifically inhibit basal secretion of FSH, but not of LH, in a rat anterior pituitary monolayer culture system. The Half-maximal effective dose for both is 2.5-6.0 ng/ml.Type: GrantFiled: July 26, 1988Date of Patent: August 20, 1991Assignee: The Salk Institute for Biological StudiesInventors: Nicholas C. K. Ling, Naoto Ueno, Shunichi Shimasaki, Frederick S. Esch, Shao-Yao Ying, Roger C. L. Guillemin
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Patent number: 4973577Abstract: A 28,000-dalton protein with FSH-releasing activity is isolated from porcine follicular fluid in a multi-step procedure including gel filtration, ion exchange chromatography and several reverse-phase high-performance liquid chromatography steps. The 28 kD protein promotes secretion of FSH, but not of LH, in a rat anterior pituitary monolayer culture system, exhibiting an EC.sub.50 of 0.5 ng/ml. These peptides are dimers of inhibin .beta.-chains of mammals, and homodimers or heterodimers of the .beta..sub.A and .beta..sub.B chains are biologically active to regulate fertility of various mammalian species, including humans.Type: GrantFiled: August 31, 1987Date of Patent: November 27, 1990Assignee: The Salk Institute for Biological StudiesInventors: Wylie W. Vale, Jr., Jean E. F. Rivier, Richard A. McClintock, Anne Corrigan, Joan Vaughan, Joachim Spiess, Nicholas C. Ling, Shao-Yao Ying, Frederick S. Esch, Roger C. L. Guillemin
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Patent number: 4740587Abstract: Two 32,000-dalton proteins with inhibin activity were isolated from porcine follicular fluid using heparin-Sepharose affinity chromatography, followed by gel filtration on Sephacryl S-200 and then four steps of reverse-phase high-performance liquid chromatography. Each isolated molecular is composed of two chains having molecular weights of about 18,000 and about 14,000 daltons, respectively, which are bound together by disulfide bonding. Microsequencing revealed the NH.sub.2 -terminal portion of the 18K chain of both to be Ser-Thr-Ala-Pro-Leu-Pro-Trp-Pro-Trp-Ser-Pro-Ala-Ala-Leu-Arg-Leu-Leu-Gln-Ar g-Pro-Pro-Glu-Glu-Pro-Ala-Val, of one of the 14K chains to be Gly-Leu-Glu-Cys-Asp-Gly-Arg-Thr-Asn-Leu-Cys-Cys-Arg-Gln-Gln-Phe-Phe-Ile-As p-Phe-Arg-Leu-Ile-Gly-Trp, and of the other 14K chain to be Gly-Leu-Glu-Cys-Asp-Gly-Lys-Val-Asn-Ile-Cys-Cys-Lys-Lys-Gln-Phe-Phe-Val-Se r-Phe-Lys-Asp-Ile-Gly-Trp-Asn-Asp-Trp-Ile-Ile-Ala-Pro.Type: GrantFiled: October 3, 1985Date of Patent: April 26, 1988Assignee: The Salk Institute for Biological StudiesInventors: Nicholas C. Ling, Shao-Yao Ying, Fred S. Esch, Roger C. L. Guillemin
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Patent number: 4610976Abstract: The invention provides synthetic peptides which are extremely potent in stimulating the release of pituitary GH in mammals and which have the formula: H-Tyr-Ala-Asp-Ala-Ile-Phe-Thr-Asn-Ser-Tyr-Arg-Lys-Val-Leu-Gly-Gln-Leu-Ser- Ala-Arg-Lys-Leu-Leu-Gln-Asp-Ile-Met-Ser-Arg-Gln-Gln-Gly-Glu-Arg-Asn-Gln-Glu -Gln-Gly-Ala-Arg-Val-Arg-Leu-Y wherein Y is OH or NH.sub.2. These peptides or biologically active fragments thereof, or analogs thereof having well-known substitutions and, or additions, as well as nontoxic salts of any of the foregoing, may be administered therapeutically to mammals, including humans, and may be used diagnostically. The peptides are useful in stimulating the release of GH and accelerating growth in warm-blooded non-human animals, particularly pigs, and in improving aquiculture.Type: GrantFiled: August 29, 1983Date of Patent: September 9, 1986Assignee: The Salk Institute for Biological StudiesInventors: Peter Bohlen, Frederick S. Esch, Nicholas C. Ling, Paul E. Brazeau, Jr., Roger C. L. Guillemin
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Patent number: 4585756Abstract: The invention provides synthetic peptides which are extremely potent in stimulating the release of pituitary GH in mammals and which have the formula: H-Tyr-Ala-Asp-Ala-Ile-Phe-Thr-Asn-Ser-Tyr-Arg-Lys-Val-Leu-Gly-Gln-Leu-Ser- Ala-Arg-Lys-Leu-Leu-Gln-Asp-Ile-Met-Asn-Arg-Gln-Gln-Gly-Glu-Arg-Asn-Gln-Glu -Gln-Gly-Ala-Lys-Val-Arg-Leu-Y wherein Y is OH or NH.sub.2. These peptides or biologically active fragments thereof, or analogs thereof having well-known substitutions and/or additions, as well as nontoxic salts of any of the foregoing, may be administered therapeutically to mammals, including humans, and may be used diagnostically. The peptides are useful in stimulating the release of GH so as to accelerate growth in warm-blooded non-human animals, particularly cattle, and/or to increase the production of milk in lactating cows, and also in improving aquiculture.Type: GrantFiled: October 12, 1983Date of Patent: April 29, 1986Assignee: The Salk Institute for Biological StudiesInventors: Paul E. Brazeau, Jr., Peter Bohlen, Frederick S. Esch, Nicholas C. Ling, Roger C. L. Guillemin
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Patent number: 4517181Abstract: PGRF has been synthesized. The invention provides synthetic peptides which are extremely potent in stimulating the release of pituitary GH in mammals and which have the formula: ##STR1## wherein R is OH or NH.sub.2, R.sub.34 is Ser or Ala, R.sub.38 is Arg or Ser, R.sub.40 is Ala or Arg and R.sub.41 is Arg, Arg-Ala, Arg-Ala-Arg, Arg-Ala-Arg-Leu or des-R.sub.41. These peptides or biologically active fragments thereof, or analogs thereof having well-known substitutions and/or additions, as well as nontoxic salts of any of the foregoing, may be administered therapeutically to mammals, including humans, and may be used diagnostically.Type: GrantFiled: September 15, 1982Date of Patent: May 14, 1985Assignee: The Salk Institute for Biological StudiesInventors: Nicholas C. Ling, Frederick S. Esch, Peter Bohlen, Paul E. Brazeau, Jr., Roger C. L. Guillemin
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Patent number: 4409139Abstract: A substantially purified substance has been isolated from bovine gonadal secretions which mediates pituitary hormone secretion, using an extraction and purification sequence that includes gel filtration, partition chromatography and HPLC in that order. The substance, designated gonadostatin, is a moderate-size peptide which below a threshold level selectively inhibits LRF-stimulated pituitary secretion of LH and FSH. Above a threshold level, gonadostatin generally stimulates pituitary hormone secretion.Type: GrantFiled: August 10, 1981Date of Patent: October 11, 1983Assignee: The Salk Institute for Biological StudiesInventors: Nicholas C. Ling, Roger C. L. Guillemin, Shao-Yao Ying, Frederick S. Esch
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Patent number: 4316891Abstract: 28-member residue and 25-member residue peptides have been synthesized containing the tetradecapeptide somatostatin that are more potent than somatostatin. Somatostatin-28 has the formula: ##STR1## The three N-terminal amino acid residues are absent in somatostatin-25. Somatostatin-28 or somatostatin-25 or a pharmaceutically acceptable addition salt thereof, dispersed in a pharmaceutically acceptable liquid or solid carrier, can be administered to mammals in the same manner as somatostatin.Type: GrantFiled: June 14, 1980Date of Patent: February 23, 1982Assignee: The Salk Institute for Biological StudiesInventors: Roger C. L. Guillemin, Nicholas C. Ling, Fred S. Esch, Peter Bohlen, Paul E. Brazeau, Jr.
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Patent number: 4280953Abstract: Somatostatin (SS) is modified to incorporate a carbohydrate moiety in the peptide chain by linkage to either Asn, Ser or Thr. The modified SS peptide analog may have the formula: ##STR1## wherein R.sub.1 is preferably a hexose or amino-hexose, such as glucose or N-acetylglucosamine. Alternatively, the carbohydrate can be linked to Ser or Thr by an ether bond. Such glycosomatostatins have an extended biological half-life compared to the parent peptide and substantially the same potency. Modifications and substitutions with respect to other amino acid residues in the chain can be made in the glycopeptides, for the purpose of increasing the effectiveness of SS analogs in other ways, and such increased effectiveness is a characteristic of the glycosomatostatin along with its longer-acting biological effect.Type: GrantFiled: November 8, 1979Date of Patent: July 28, 1981Assignee: The Salk Institute for Biological StudiesInventors: Roger C. L. Guillemin, Solange Lavielle, Paul E. Brazeau, Jr., Nicholas C. Ling, Robert A. Benoit