Abstract: Purified cartilage and/or bone inductive proteins and processes for producing them are disclosed. The proteins may be used in the treatment of bone and/or cartilage defects and in wound healing and related tissue repair.

Abstract: Novel polypeptides of human megakaryocyte stimulating factors (MSFs). Pharmaceutical compositions containing same, and methods for their preparation and use are provided.

Abstract: The method of the invention provides novel compounds, termed acid-labile isotope-coded extractants (ALICE), for quantitative mass spectrometric analysis of protein mixtures. The compounds contain a thiol-reactive group that is used to capture cysteine-containing peptides from all peptide mixtures, an acid-labile linker, and a non-biological polymer. One of the two acid-labile linkers is isotopically labeled and therefore enables the direct quantitation of peptides/proteins through mass spectrometric analysis. Because no functional proteins are required to capture peptides, a higher percentage of organic solvent can be used to solubilize the peptides, particularly hydrophobic peptides, through the binding, washing and eluting steps, thus permitting much better recover of peptides. Moreover, since the peptides are covalently linked to the non-biological polymer (ALICE), more stringent washing is allowed in order to completely remove non-specifically bound species.

Abstract: Novel polypeptides of human megakaryocyte stimulating factors (MSFs). Pharmaceutical compositions containing same, and methods for their preparation and use are provided.

Abstract: Arginine-containing cysteine-modifying compounds useful for MALDI-MS analysis of proteins are provided. These compounds termed isotope-coded ionization enhancement reagents (ICIER) can provide ionization enhancement in MALDI-MS, relative quantitation, and additional database searching constraints at the same time without any extra sample manipulation. More specifically, ICIER increase the ionization efficiency of cysteine-containing peptides by attachment of a guanidino functional group. ICIER also increase the overall hydrophilicity of these peptides due to the hydrophilic nature of ICIER and thus increase the percentage of recovery of these peptides during sample handling and processing such as in-gel digestion or liquid chromatography.

Abstract: The method of the invention provides novel compounds, termed acid-labile isotope-coded extractants (ALICE), for quantitative mass spectrometric analysis of protein mixtures. The compounds contain a thiol-reactive group that is used to capture cysteine-containing peptides from all peptide mixtures, an acid-labile linker, and a non-biological polymer. One of the two acid-labile linkers is isotopically labeled and therefore enables the direct quantitation of peptides/proteins through mass spectrometric analysis. Because no functional proteins are required to capture peptides, a higher percentage of organic solvent can be used to solubilize the peptides, particularly hydrophobic peptides, through the binding, washing and eluting steps, thus permitting much better recovery of peptides. Moreover, since the peptides are covalently linked to the non-biological polymer (ALICE), more stringent washing is allowed in order to completely remove non-specifically bound species.

Abstract: Arginine-containing cysteine-modifying compounds useful for MALDI-MS analysis of proteins are provided. These compounds termed isotope-coded ionization enhancement reagents (ICIER) can provide ionization enhancement in MALDI-MS, relative quantitation, and additional database searching constraints at the same time without any extra sample manipulation. More specifically, ICIER increase the ionization efficiency of cysteine-containing peptides by attachment of a guanidino functional group. ICIER also increase the overall hydrophilicity of these peptides due to the hydrophilic nature of ICIER and thus increase the percentage of recovery of these peptides during sample handling and processing such as in-gel digestion or liquid chromatography.

Abstract: The method of the invention provides novel compounds, termed acid-labile isotope-coded extractants (ALICE), for quantitative mass spectrometric analysis of protein mixtures. The compounds contain a thiol-reactive group that is used to capture cysteine-containing peptides from all peptide mixtures, an acid-labile linker, and a non-biological polymer. One of the two acid-labile linkers is isotopically labeled and therefore enables the direct quantitation of peptides/proteins through mass spectrometric analysis. Because no functional proteins are required to capture peptides, a higher percentage of organic solvent can be used to solubilize the peptides, particularly hydrophobic peptides, through the binding, washing and eluting steps, thus permitting much better recovery of peptides. Moreover, since the peptides are covalently linked to the non-biological polymer (ALICE), more stringent washing is allowed in order to completely remove non-specifically bound species.

Abstract: Novel polypeptides of human megakaryocyte stimulating factors (MSFs). Pharmaceutical compositions containing same, and methods for their preparation and use are provided.

Abstract: Novel human megakaryocyte stimulating factors (MSFS) capable of stimulating the growth and development of colonies of megakaryocytes, pharmaceutical compositions containing same, and methods for their preparation and use are provided.

Abstract: Purified cartilage and/or bone inductive proteins and processes for producing them are disclosed. The proteins may be used in the treatment of bone and/or cartilage defects and in wound healing and related tissue repair.

Abstract: A novel human megakaryocytopoietic factor capable of stimulating the growth and development of colonies of megakaryocytes is provided, including procedures for its purification and use as a pharmaceutical agent.

Abstract: A method for purifying erythropoietin is described. The method comprises treating partially purifying erythropoietin by reverse phase high performance liquid chromatography to obtain homogeneous erythropoietin having a molecular weight of about 34,000 daltons on SDS PAGE and moving a single peak on reverse phase HPLC. The homogeneous erythropoietin protein preferably has a specific activity of at least 120,000 IU, more preferably at least 160,000 IU per absorbance unit at 280 nm.

Abstract: An improved apparatus and method for the sequential performance of chemical processes on a sample of chemical material wherein the sample is embedded in a solid matrix of fluid permeable material located within a reaction chamber and is sequentially subjected to a plurality of fluids passed through the chamber in a pressurized stream, causing chemical interaction between the sample and the fluids.

Abstract: A method for purifying erythropoietin is described. The method comprises treating partially purifying erythropoietin by reverse phase high performance liquid chromatography to obtain homogeneous erythropoietin having a molecular weight of about 34,000 daltons on SDS PAGE and moving a single peak on reverse phase HPLC. The homogeneous erythropoietin protein preferably has a specific activity of at least 120,000 IU, more preferably at least 160,000 IU per absorbance unit at 280 nm.

Abstract: Conversion flask for use is an apparatus for the sequential performance of chemical processes on a sample of chemical material. The flask includes at least three capillary tubes and a large bore tube extending into the interior thereof for the introduction and withdrawal of various fluids. The capillary tubes are constructed to introduce a plurality of fine bubbles into a liquid within the flask to agitate the liquid and accelerate drying, to impinge chemicals on the walls of the flask, and to produce a spray onto the interior walls of the flask in proximity to its upper end to wash down the interior walls of the flask.

Abstract: An improved method for the sequential performance of chemical processes on a sample of chemical material wherein the sample is embedded in a solid matrix of fluid permeable material located within a reaction chamber and is sequentially subjected to a plurality of fluids passed through the chamber in a pressurized stream, causing chemical interaction between the sample and the fluids.