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Biomedical subjects

S BERMAN

Publications and source records attributed to S BERMAN.

At least 19 recordsLinked to original sources
PubMed1963

BACTERIAL VACCINE IN MULTIDOSE TABLET FORM FOR PARENTERAL USE.

Dried typhoid vaccines were prepared by freeze-drying of heat-inactivated phenolized-cell suspensions and by an acetone-killed and dried technique. Portions of the dried powder obtained by each method were compressed into tablets. Tests with the products showed that drying and making of tablets did not affect the ability of the vaccines to protect mice or elicit antibodies in rabbits.

Acetone↗
PubMed1962

Enzymatic debridement of third-degree burns on guinea pigs by Clostridium histolyticum proteinases.

Webster, Marion E. (Walter Reed Army Institute of Research, Washington, D. C.), Patricia L. Altieri, David A. Conklin, Sanford Berman, Joseph P. Lowenthal, and Raymond B. Gochenour. Enzymatic debridement of third-degree burns on guinea pigs by Clostridium histolyticum proteinases. J. Bacteriol. 83:602-608. 1962.-An attempt has been made to correlate in vitro activities of Clostridium histolyticum H-4 proteinases, as measured against azocasein, azocoll, gelatin, and collagen, with their ability to debride full-thickness third-degree burns (360 C, 15 sec) on guinea pigs. The major portion of the debriding activity is tentatively identified as due to the delta-proteinase, in the absence of cysteine, and to a new proteinase contained in the same fraction in the presence of cysteine. Other proteinases produced by this strain were also capable of debriding burns. However, collagenase and the gelatinase of the 0 to 22% fraction did not appear to be essential for the debridement of these burns.Studies of the proteinases produced by this organism have suggested that at least nine and probably more proteolytic enzymes are present. The need for more highly purified proteinases, in order to determine which enzyme(s) is responsible for debridement of guinea pig burns, is evident.

Animals↗
PubMed1961

Eastern equine encephalomyelitis vaccine prepared in cell cultures.

Protection tests in guinea pigs indicate that vaccines prepared from virus propagated in chick embryo cell cultures are as effective as the purified whole chick embryo vaccines which are currently used for human immunization against eastern equine encephalomyelitis.

Animals↗
PubMed1961

Factors affecting the elaboration by Clostridium histolyticum of proteinases capable of debriding third degree burn eschars on guinea pigs.

Berman, Sanford (Walter Reed Army Institute of Research, Washington, D. C.), Joseph P. Lowenthal, Marion E. Webster, Patricia L. Altieri, and Raymond B. Gochenour. Factors affecting the elaboration by Clostridium histolyticum of proteinases capable of debriding third degree burn eschars on guinea pigs. J. Bacteriol. 82:582-588. 1961.-A comparison of three strains of Clostridium histolyticum grown in two different media indicated that the H-4 strain produced the greatest yield of enzyme(s) capable of debriding third degree burn eschars on guinea pigs. Some of the nutritional and physiological factors affecting the elaboration of enzymes by this strain have been investigated. Maximal yields have been obtained after incubation for 14 to 16 hr at 30 C in a medium consisting of 5% proteose-peptone, 1.5% trypticase soy broth, and vitamins; pH 7.5. A medium consisting of 2% proteose-peptone and 2% Casamino acids yields somewhat lower enzyme titers, but has the compensating advantage of being less costly and may be more amenable to purification and concentration procedures because of its reduced precipitable nitrogen content.

Amino Acids↗
PubMed1961

Large scale purification of proteinases from Clostridium histolyticum filtrates.

Conklin, David A. (Walter Reed Army Institute of Research, Washington, D. C.), Marion E. Webster, Patricia L. Altieri, Sanford Berman, Joseph P. Lowenthal, and Raymond B. Gochenour. Large scale purification of proteinases from Clostridium histolyticum filtrates. J. Bacteriol. 82:589-594. 1961.-A method for the large scale preparation and partial purification of Clostridium histolyticum proteinases by fractional precipitation with ammonium sulfate is described. Conditions for adequate separation and purification of the delta-proteinase and the gelatinase were obtained. Collagenase, on the other hand, was found distributed in four to five fractions and little increase in purity was achieved as compared to the crude ammonium sulfate precipitates.

Clostridium↗