US4599318A — Tissue protein PP19, a process for obtaining it, …

Claim 1

Independent Claim 168 words

A protein PP 19 extracted from a source of said protein and having the following characteristics: (a) an electrophoretic mobility in the region between that of α 1 and of β 1 globulins; (b) an isoelectric point between 4.6 and 5.4; (c) a sedimentation coefficient s 20 ,w of 3.25±0.25 S; (d) a molecular weight determined in the ultracentrifuge of 36,500±4,000; (e) a carbohydrate fraction of 3.9±1.5 g/100 g (mannose 0.3±0.2, fucose 0.2±0.1, galactose 1.0±0.3, glucose 0.4±0.2, N-acetylglucosamine 1.2±0.3, N-acetylgalactosamine 0.1±0.1, and N-acetylneuraminic acid 0.7±0.3, each g/100 g); and (f) an amino acid composition as in the following table: ______________________________________ Residues per Coefficient of Amino acid 100 residues variation ______________________________________ lysine 8.63 2.92 histidine 1.71 14.20 arginine 2.73 7.71 aspartic acid 11.51 3.99 threonine 4.20 15.75 serine 7.48 2.26 glutamic acid 11.09 3.20 proline 4.12 18.29 glycine 6.88 5.12 alanine 7.56 3.30 cystine 1/2 2.10 22.58 valine 7.44 3.98 methionine 2.39 7.24 isoleucine 3.40 6.38 leucine 10.03 7.29 tyrosine 2.19 2.96 phenylalanine 5.05 2.58 tryptophan 1.42 15.43 ______________________________________

Claim 2

Dependent Claim 168 words

A protein PP 19 extracted from a source of said protein and having the following characteristics: (a) an electrophoretic mobility in the region between that of α 1 and of β 1 globulins; (b) an isoelectric point between 4.6 and 5.4; (c) a sedimentation coefficient s 20 ,w of 3.25±0.25 S; (d) a molecular weight determined in the ultracentrifuge of 36,500±4,000; (e) a carbohydrate fraction of 3.9±1.5 g/100 g (mannose 0.3±0.2, fucose 0.2±0.1, galactose 1.0±0.3, glucose 0.4±0.2, N-acetylglucosamine 1.2±0.3, N-acetylgalactosamine 0.1±0.1, and N-acetylneuraminic acid 0.7±0.3, each g/100 g); and (f) an amino acid composition as in the following table: ______________________________________ Residues per Coefficient of Amino acid 100 residues variation ______________________________________ lysine 8.63 2.92 histidine 1.71 14.20 arginine 2.73 7.71 aspartic acid 11.51 3.99 threonine 4.20 15.75 serine 7.48 2.26 glutamic acid 11.09 3.20 proline 4.12 18.29 glycine 6.88 5.12 alanine 7.56 3.30 cystine 1/2 2.10 22.58 valine 7.44 3.98 methionine 2.39 7.24 isoleucine 3.40 6.38 leucine 10.03 7.29 tyrosine 2.19 2.96 phenylalanine 5.05 2.58 tryptophan 1.42 15.43 ______________________________________

Claim 3

Dependent Claim 194 words

A process for obtaining or enriching PP 19 as claimed in claim 1, which comprises subjecting an extract which has been obtained, using a dilute salt or buffer solution or a solution of a solubilizing agent, from at least one organ which contains this protein PP 19 to one or more of the following measures: (a) Precipitation of the protein PP 19 with ammonium sulfate in the pH range of 5 to 8 and at 30-70% saturation; (b) Precipitation of the protein PP 19 using a water-soluble acridine base at a pH of 8 to 9 and a concentration of the base of 4-8 g/l; (c) Separation out of part of the accompanying proteins by addition of ethanol at pH 7 up to a final concentration of 200 ml/l alcohol; (d) Preparative zone electrophoresis, where the protein fraction between α 1 and β 2 globulins is obtained; (e) Gel filtration or ultrafiltration where proteins in the molecular weight range of 20,000 to 60,000 are obtained; (f) Adsorption onto a weakly basic ion exchanger and elution of the protein PP 19 ; and (g) Enrichment by immunoadsorption, to obtain or enrich said PP 19 protein.

Claim 4

Dependent Claim 37 words

The process of claim 2, wherein said organ is selected from the group consisting of placenta, stomach and spleen, wherein said buffer solution is a glycine HCl buffer and wherein said solubilizing agent is a urea solution.

Claim 5

Dependent Claim 45 words

A process for isolating the protein PP 19 of claim 1 comprising the steps of subjecting a liquid containing said protein PP 19 to at least one known procedure for isolating proteins and, in each instance, recovering that material containing said protein PP 19 .

Claim 6

Dependent Claim 20 words

The protein PP 19 of claim 1, said protein being extracted from an organ or an extract of an organ.

Claim 7

Dependent Claim 20 words

The protein PP 19 of claim 5, said protein being extracted from a placenta or an extract of a placenta.

Claim 8

Dependent Claim 12 words

The protein PP 19 of claim 6, said protein being substantially pure.

Claim 9

Dependent Claim 24 words

An antiserum to the protein PP 19 of claim 1 obtained by immunizing an animal with said protein PP 19 and recovering said antiserum.

Claim 10

Dependent Claim 23 words

A method for detecting and determining protein PP 19 comprising the step of utilizing an effective amount of the antiserum of claim 8.

Claim 11

Dependent Claim 159 words

A substantially pure protein PP 19 , with the following characteristics: (a) an electrophoretic mobility in the region between that of α 1 and of β 1 globulins; (b) an isoelectric point between 4.6 and 5.4; (c) a sedimentation coefficient s 20 ,w of 3.25±0.25 S; (d) a molecular weight determined in the ultracentrifuge of 36,500±4,000; (e) a carbohydrate fraction of 3.9±1.5 g/100 g (mannose 0.3±0.2, fucose 0.2±0.1, galactose 1.0±0.3, N-acetylglucosamine 1.2±0.3, and N-acetylneuraminic acid 0.7±0.3, each g/100 g); and (f) an amino acid composition as in the following table: ______________________________________ Residues per Coefficient of Amino acid 100 residues variation ______________________________________ lysine 8.63 2.92 histidine 1.71 14.20 arginine 2.73 7.71 aspartic acid 11.51 3.99 threonine 4.20 15.75 serine 7.48 2.26 glutamic acid 11.09 3.20 proline 4.12 18.29 glycine 6.88 5.12 alanine 7.56 3.30 cystine 1/2 2.10 22.58 valine 7.44 3.98 methionine 2.39 7.24 isoleucine 3.40 6.38 leucine 10.03 7.29 tyrosine 2.19 2.96 phenylalanine 5.05 2.58 tryptophan 1.42 15.43 ______________________________________

Claim 12

Dependent Claim 159 words

A substantially pure protein PP 19 , with the following characteristics: (a) an electrophoretic mobility in the region between that of α 1 and of β 1 globulins; (b) an isoelectric point between 4.6 and 5.4; (c) a sedimentation coefficient s 20 ,w of 3.25±0.25 S; (d) a molecular weight determined in the ultracentrifuge of 36,500±4,000; (e) a carbohydrate fraction of 3.9±1.5 g/100 g (mannose 0.3±0.2, fucose 0.2±0.1, galactose 1.0±0.3, N-acetylglucosamine 1.2±0.3, and N-acetylneuraminic acid 0.7±0.3, each g/100 g); and (f) an amino acid composition as in the following table: ______________________________________ Residues per Coefficient of Amino acid 100 residues variation ______________________________________ lysine 8.63 2.92 histidine 1.71 14.20 arginine 2.73 7.71 aspartic acid 11.51 3.99 threonine 4.20 15.75 serine 7.48 2.26 glutamic acid 11.09 3.20 proline 4.12 18.29 glycine 6.88 5.12 alanine 7.56 3.30 cystine 1/2 2.10 22.58 valine 7.44 3.98 methionine 2.39 7.24 isoleucine 3.40 6.38 leucine 10.03 7.29 tyrosine 2.19 2.96 phenylalanine 5.05 2.58 tryptophan 1.42 15.43 ______________________________________

Claim 13

Dependent Claim 56 words

A method of diagnosing or monitoring a disease or monitoring the treatment of said disease, said disease being accompanied by an increase in the concentration of protein PP 19 , comprising the step of utilizing in an immunochemical method the protein PP 19 of claim 1 to achieve said intended purpose with respect to said disease.

Annuity Stage	Window Opens	Payment Deadline	Surcharge Period Until	Estimated Fee	Status
3.5 Years (Year 4)	1989-07-07	1990-01-06	1990-07-08	$2000.00	Window Closed / Lapsed
7.5 Years (Year 8)	1993-07-07	1994-01-06	1994-07-08	$3760.00	Window Closed / Lapsed
11.5 Years (Year 12)	1997-07-07	1998-01-06	1998-07-08	$7700.00	Window Closed / Lapsed

Tissue protein PP19, a process for obtaining it, and its use

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