33 results match your criteria: "and the Hospital of The Rockefeller Institute for Medical Research[Affiliation]"

A STUDY OF THE INHIBITION OF STREPTOCOCCAL PROTEINASE BY SERA OF NORMAL AND IMMUNE ANIMALS AND OF PATIENTS INFECTED WITH GROUP A HEMOLYTIC STREPTOCOCCI.

J Exp Med

May 1947

Belmont Laboratories (London County Council), Sutton, Surrey, The Serum Institute, (Wellcome Foundation), Carshalton, Surrey, England, and the Hospital of The Rockefeller Institute for Medical Research, New York.

Antiproteinase sera were prepared by immunizing horses with filtrates from a selected strain of group A streptococcus. This strain, which produced high titred proteinase but no erythrogenic toxin, was selected from forty-two strains of group A streptococci which produced varying amounts of proteinase. A few strains belonging to groups B, C, and G were also tested; they were all proteinase-negative.

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Studies on LS-protein, the soluble double antigen of vaccinia, and on the degradation products L'S and L''S' have been made with electrophoresis and in the analytical ultracentrifuge. LS, which is homogeneous electrically and in the ultracentrifuge, has an isoelectric point at pH 4.8.

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Virus-free filtrate, obtained from suspensions of vaccine virus-infected dermal pulp of rabbits and rich in the soluble substances of vaccinia, was shown to contain four distinct components in electrophoresis experiments. Electrophoretic and serological observations served as a guide in developing a method for separating these components from one another. This method depended upon changes in the solubilities of the components with alterations of pH.

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Electrophoretic studies were made on vaccine virus, collodion particles, and glass particles suspended in 0.01 molar buffer solutions at pH 7.9, in which the moving boundary method was used.

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Ultracentrifugal studies on the CL dermal strain of vaccine virus indicate the following characteristics of the elementary bodies:- 1. A stable suspension of Paschen bodies in a dilute buffer solution of pH 6.2 to 8 sediments with the formation of a characteristic primary boundary which consistently shows a spread of approximately 14 per cent.

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THE ABSENCE FROM THE URINE OF PERNICIOUS ANEMIA PATIENTS OF A MOSQUITO GROWTH FACTOR PRESENT IN NORMAL URINE.

J Exp Med

February 1938

Department of Animal and Plant Pathology, The Rockefeller Institute for Medical Research, Princeton, New Jersey, and the Hospital of The Rockefeller Institute for Medical Research, New York.

Extracts prepared from the urine of normal persons or patients with aplastic anemia or leukemia contain a substance, possibly flavine or a flavine compound, which under suitable conditions of test enhances the growth of larvae of the mosquito, Aëdes aegypti. This substance is lacking, or is present in much smaller amount, in extracts from the urine of pernicious anemia patients showing symptoms of the disease. Extracts from the urine of the same patients after adequate treatment contain as much of the substance as normal urine extracts.

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THE SUSCEPTIBILITY OF SWINE TO THE VIRUS OF HUMAN INFLUENZA.

J Exp Med

October 1936

Department of Animal and Plant Pathology, The Rockefeller Institute for Medical Research, Princeton, N. J., and the Hospital of The Rockefeller Institute for Medical Research, New York.

Swine inoculated intranasally with human influenza virus alone develop an ill defined, mild, and usually afebrile illness of short duration. At postmortem the anterior lobes of the lungs of such animals contain scant, scattered areas of lobular atelectasis. Transmission of the virus for 5 serial passages through two groups of swine failed noticeably to enhance its pathogenicity for this species.

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Washed elementary bodies obtained from dermal vaccine virus contain ash, carbohydrate, fat, and nitrogen a part of which is undoubtedly in the form of protein. These components are similar to those found in bacteria and other substances of protoplasmic origin.

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Intravenous inoculation of small doses of non-hemolytic streptococci into previously sensitized rabbits is usually followed by the appearance of perivascular cellular aggregates in lung and liver. The characteristic cell in these aggregates is moderately large, with vesicular nucleus, prominent nucleoli, clumped chromatin, and basophilic cytoplasm. In addition, the lesions contain small lymphocytes and granulocytes.

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The denaturation of hemoglobin by salicylate in neutral solution is completely reversible. There is a mobile equilibrium between native and denatured hemoglobin in neutral salicylate solution. The higher the salicylate concentration the greater is the percentage denaturation.

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THE EQUILIBRIUM BETWEEN ACTIVE NATIVE TRYPSIN AND INACTIVE DENATURED TRYPSIN.

J Gen Physiol

January 1934

Laboratories of The Rockefeller Institute for Medical Research, Princeton, N. J., and the Hospital of The Rockefeller Institute for Medical Research, New York.

There is a mobile equilibrium between the native and denatured forms of trypsin which depends on the concentrations of acid, alkali, and alcohol and on the temperature. The heat of denaturation in 0.01 N hydrochloric acid calculated from the effect of temperature on the equilibrium constant is -67,600 calories per mole.

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THE ESTIMATION OF ACTIVE NATIVE TRYPSIN IN THE PRESENCE OF INACTIVE DENATURED TRYPSIN.

J Gen Physiol

November 1933

Laboratories of The Rockefeller Institute for Medical Research, Princeton, N. J., and the Hospital of The Rockefeller Institute for Medical Research, New York.

Inactive denatured trypsin changes into active native trypsin in the protein solutions which have been used to estimate tryptic activity. If the digestion mixture, however, is alkaline enough and contains enough urea this change does not take place. Such a digestion mixture can be used to estimate active native trypsin in the presence of inactive denatured trypsin.

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THE ESTIMATION OF TRYPSIN WITH HEMOGLOBIN.

J Gen Physiol

November 1933

Laboratories of The Rockefeller Institute for Medical Research, Princeton, N. J., and the Hospital of The Rockefeller Institute for Medical Research, New York.

The formation from hemoglobin of split products not precipitable by trichloracetic acid is taken as a measure of tryptic activity. The split products are estimated colorimetrically. Many measurements of tryptic activity can be made in a short time and different samples of hemoglobin yield the same results.

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THE ESTIMATION OF PEPSIN WITH HEMOGLOBIN.

J Gen Physiol

September 1932

Laboratories of The Rockefeller Institute for Medical Research, Princeton, N. J., and the Hospital of The Rockefeller Institute for Medical Research, New York.

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THE EFFECT OF DENATURATION ON THE VISCOSITY OF PROTEIN SYSTEMS.

J Gen Physiol

January 1932

Laboratories of The Rockefeller Institute for Medical Research, Princeton, N. J., and the Hospital of The Rockefeller Institute for Medical Research, New York.

The viscosity of a protein solution is increased by the denaturation of the protein. This is true both when there is the formation of protein aggregates which occlude water and when there is no aggregation. Under certain conditions, as a result of the aggregation following denaturation, a solution containing only one per cent of protein may be converted into a clear gel.

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PROTEIN COAGULATION AND ITS REVERSAL : SERUM ALBUMIN.

J Gen Physiol

July 1931

Laboratories of The Rockefeller Institute for Medical Research, Princeton, N. J., and the Hospital of The Rockefeller Institute for Medical Research, New York.

1. It is possible to prepare crystalline, soluble, heat-coagulable serum albumin from coagulated serum albumin. 2.

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PROTEIN COAGULATION AND ITS REVERSAL : GLOBIN.

J Gen Physiol

May 1931

Laboratories of The Rockefeller Institute for Medical Research, Princeton, N. J., and the Hospital of The Rockefeller Institute for Medical Research, New York.

1. The globin prepared from hemoglobin by the acid acetone method is denatured globin. 2.

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1. Methemoglobin prepared from coagulated hemoglobin by the reversal of coagulation has the same solubility within 2 per cent as normal methemoglobin. 2.

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THE REACTIONS OF CYANIDE WITH GLOBIN HEMOCHROMOGEN.

J Gen Physiol

September 1930

Laboratories of The Rockefeller Institute for Medical Research, Princeton, N. J., and the Hospital of The Rockefeller Institute for Medical Research, New York, N. Y.

Cyanide can react with globin hemochromogen in two different ways. In the first reaction cyanide combines with globin hemochromogen without displacing or competing with globin. In the second reaction cyanide displaces globin.

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1. By a procedure involving the use of acid acetone hemoglobin may be rapidly separated into a precipitate of denatured globin and an acetone solution of heme. 2.

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THE PREPARATION OF COMPLETELY COAGULATED HEMOGLOBIN.

J Gen Physiol

November 1929

Laboratories of The Rockefeller Institute for Medical Research, Princeton, N. J., and the Hospital of The Rockefeller Institute for Medical Research, New York, N. Y.

As a preliminary to the study of the reversal of the coagulation of hemoglobin several methods are described for the preparation of completely denatured and coagulated hemoglobin and the evidence is given that hemoglobin is a typical coagulable protein.

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1. Biological effects of electromagnetic waves emitted by a vacuum tube oscillator have been studied at frequencis ranging from 8,300,000 to 158,000,000 cycles per second (1.9 to 38 meters wave-length).

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