ROBERT A ROSENBERG
Broker in Brookline, MA

5155211, Oct 13, 1992

Nov 16, 1989

7/437544

Robert D. Rosenberg - Brookline MA

Massachusetts Institute of Technology - Cambridge MA

C07K 1500

530351

A megakaryocyte stimulatory factor (MSF), purified to homogeneity, is an acidic protein (pI=5. 1) with an Mr=15,000 which stimulates PF4-like protein synthesis in rat promegakaryoblast cells by as much as 7-fold, and exhibits half-maximal activity at a concentration of 0. 8 pM. MSF exhibits no biologic activity corresponding to other known hemopoietic growth factors, and appears to be specific for the megakaryocyte lineage. In the given examples, MSF was purified to homogeneity (as judged by SDS-PAGE and isoelectric focusing in the presence of 9. 2 M urea) from serum-free conditioned medium obtained from cultured human embryonic kidney (HEK) cells, and to near homogeneity from thrombocytopenic plasma. The MSF is isolated by precipitating the MSF with ammonium sulfate at 80% saturation, removing insoluble, non-MSF material and applying the soluble protein to a WGA-Sepharose column, eluting the MSF protein with chitin oligosaccharides, applying the concentrated eluant containing MSF activity to a Biogel P200 column, and chromatographing the eluted MSF fractions on a TSK-G3000 HPLC size exclusion column.

4945054, Jul 31, 1990

May 17, 1983

6/495511

Christine Fougnot - Saint Denis, FR
Marcel Jozefowicz - Lamorlaye, FR
Robert D. Rosenberg - Brookline MA

Commissariat a l'Energie Atomique - Paris

C12N 974, C12N 948

435214

The present invention relates to a process for separating and purifying proteases and antiproteases. This process is characterized in that there are placed in contact an insoluble cross-linked polymer including in its chain the group --SO. sub. 3 R. sub. 1 -- and/or the group --SO. sub. 2 R. sub. 2 -- in which R. sub. 1 denotes a hydrogen atom or metal and R. sub. 2 denotes the remainder of an amino acid linked to the --SO. sub. 2 -- bridge through its amine --NH--, function, with the solution containing proteases and antiproteases or their complex; separating the polymer which has absorbed the desired protein, washing it carefully with the buffer, desorbing the absorbed protein by a solution of a polycationic compound in the case of T or by an albumin solution in the case of AT or of the complex T-AT, and isolating the protein, if desired, by known means, such as, especially, freeze drying. The invention is useful for studying the mechanism of blood coagulation.

4539398, Sep 3, 1985

Jan 9, 1984

6/569551

Robert D. Rosenberg - Brookline MA

Riker Laboratories, Inc. - St. Paul MN

C08B 3710

536 21

A highly discriminating technique utilizing Concanavalin A, immobilized on a solid substrate, e. g. sepharose 4B, for the fractionation of heparin is disclosed. The heparin to be fractionated is incubated with antithrombin whereby a fraction complete with the antithrombin and the whole is then either passed through a column of the immobilized Concanavalin A or slurried with same. In both modes that fraction of the heparin complexed with the antithrombin is selectively absorbed by the immobilized Concanavalin A and constitutes the anticoagulant active fraction. That heparin which complexes with the antithrombin can be further fractionated to yield yet more highly active fractions by complexing the heparin in stages, adding an increment of a molar amount of antithrombin in each stage. A high molecular weight fraction (18,000-22,000 daltons) or a low molecule weight fraction (6,000-8,000 daltons), isolated from the heparin of animal tissue origin by chromatography, are the preferred heparin preparations for complexing with the antithrombin.

5536636, Jul 16, 1996

Feb 28, 1994

8/202389

Robert M. Freeman - Boston MA
Jorge Plutzky - Boston MA
Benjamin G. Neel - Wayland MA
Robert D. Rosenberg - Brookline MA

Beth Israel Hospital - Boston MA
Massachusetts Institute of Technology - Cambridge MA

C07H 2164, C12P 1934, C12Q 168

435 6

The present invention relates to the isolation of genes encoding novel protein tyrosine phosphatases (PTPs) having SH2 domains, the nucleic acid sequences isolated, and the encoded phosphatases. The invention further relates to methods of altering tyrosine phosphatase activities encoded by the novel phosphatases. By altering (i. e. , increasing or decreasing) tyrosine phosphatase activity, one can alter megakaryocyte cell function, and thereby alter platelet production. Alteration of the genes is associated with neoplastic disease.

4301153, Nov 17, 1981

Mar 30, 1978

5/891706

Robert D. Rosenberg - Brookline MA

Riker Laboratories, Inc. - St. Paul MN

A61K 3514, A61K 31725, C08B 3710

424183

A heparin preparation which exhibits elevated anticoagulant activity and a process for producing the preparation. Conventional heparin exhibiting characteristic anticoagulant activity and molecular heterogeneity is incubated with antithrombin-heparin cofactor extracted from plasma. A portion of the heparin forms a complex with the cofactor. The uncomplexed heparin fraction is then separated from the complexed fraction, and the complexed fraction is broken down to produce cofactor and an active form of heparin.