480 PATENT ABSTRACTS

dead cells in mixed populations of cells. Ac- quired resistance to immune effectors used in therapy may be determined and used to identify methods to circumvent such resistance using the method.

4996296

C R O M O L Y N B I N D I N G P R O T E I N IN H I G H L Y P U R I F E D F O R M ,

A N D M E T H O D S F O R T H E I S O L A T I O N T H E R E O F

4996146

R A P I D S T E R I L I Z A T I O N E N Z Y M A T I C P R O C E S S W I T H

P E R S I S T E N C E

Jack Kessler

An enzymatic sterilization system is disclosed which is effective against viruses and other or- ganisms. Methods are disclosed to increase the rate of and reduce the cost for sterilization with this chemistry as compared to the prior art. Methods are disclosed to formulate a sterlizing chemistry which actively maintains a sterile en- vironment over a defined period of time.

Israel Peeht, Stefan Hemmerich, Rehovot, Israel assigned to Yeda Research & Development Co Ltd

Substantially pure cromolyn binding protein is prepared by means of affinity chromatography of cromolyn derivatives bound to insoluble matrices. Aminocromolyn is prepared by a six- step synthesis and amine derivatives thereof are prepared by conventional means. Obtaining a compound having an amine group instead of the OH group at the 2-carbon of the propane link of cromolyrl permits many kinds of reactions without interfering with the portion of the cromolyn molecule with causes its pharma- cological activity. The cromolyn derivatives can be conjugated to proteins such as BSA by means of glutaraldehyde cross-linking and such con- jugates can be covalently bound to agarose beads. Cromolyn binding protein can be isolated by passing lysates of RBL-2H3 cells through chromatographic columns packed with such beads. The cromolyn binding protein can be fur- ther purified by means of lectin-agarose columns.

4996150

B I O C A T A L Y S T I M M O B I L I Z A T I O N IN A G E L O F

A N I O N I C P O L Y S A C C H A R I D E A N D C A T I O N I C P O L Y M E R

John Joung, Cavil Akin, Garfield Royer as- signed to Amoco Corporation

An immobilized biocatalyst suitable for fermen- ting to produce ethanol is prepared by mixing a biocatalyst such as a microorganism with a reac- tion product of a homogeneous dispersion of an anionic poly~ccharide such as alginate and a cationic polymer such as polyethyleneimine, and combining the resultant dispersion with an oil phase to form beads. A surtactant may be pre- sent when combining the dispersion with the oil phase. A water soluble-oil insoluble curing pow- der includinga salt of a multivalent cation such as calcium chloride is mixed with the beads in the oil phase to gell and dehydrate the beads and to prevent the beads from adhering to one another until individual bead surfaces become hardened.

4996343

S T A B L E S I L I C A - B A S E D E T H E R B O N D E D P H A S E S F O R

B I O P O L Y M E R S E P A R A T I O N S

Barry L Karger, Binyamin Feibush, Neil T Mil- ler, Alvaro Figueroa assigned to Northeastern University

Fast high resolution separations of biopolymers with retention of biological activity have been achieved by hydrophobic interaction chromatography using trialkoxy silyl ethers of the general formula See Patent Jbr Tabular Pre- sentation PS chemically bonded to silica-based chromatographic supports. In the formula R is alkyl of from one to five carbons, m is an integer from two to five, n is an integer from one to five, p is an integer from zero o f ten, and R" is methyl. phenyl, or substituted phenyl. Stable and

PATENT ABSTRACTS

reproducible bonded phases are prepared in a novel solventless procedure by a bonding pro- cess which uses a defined and controlled amount of water on the silica surface and a gaseous or volatile basic catalyst such as ammonia to pro- duce a controlled amount of silane polymeriza- tion and cross-linking in addition to extensive bonding between silane and silica. High perfor- mance liquid chromatography on such weakly hydrophobic stationary phases using aqueous eluents and decreasing salt gradients under mild conditions permits high speed, high resolution separations of biopolymers such as proteins without destruction of their biological activity and without column degradation. Size exclusion chromatography can also be performed on these phases using low ioinic strength eluents.

481

American tree Phyllanthus acuminatus and is herein designated Phyllanthostatin A. Separa- tion of a methanol extract of the root by size ex- clusion chromatography, high speed countercurrent distribution and semi- preparative hplc afforded glycoside in 0.007% yield. In solution, phyllanthostatin A was slowly transformed into justicidin-B. The structure of the lignan glycoside, determined by hrfabms and 2D nmr spectroscopy, is: See Patent for Chem- ical SIructure

4997916

4 9 9 7 7 ~

P R O C E S S F O R R E C O V E R I N G L - A M I N O A C I D S F R O M

F E R M E N T A T I O N L I Q U O R S C O N T A I N I N G T H E M

Masashi Miyazawa, Toyokazu Kaneko, Tet- suya Kaneko, Kenich Yarita, Shigenori Mori, Kinzo litani, Masaki Yamamoto, Yokohama, Japan assigned to Ajinomoto Co Inc

A process for recovering a high-purity L-amino acid from a fermentation liquor obtained by fer- mentation or an enzymic method, which com- prises removing the impurities contained in said fermentation liquor by passing said fermenta- tion liquor through an ultrafilter membrane and then through an ion-exchange or adsorbent resin; concentrating or cooling the effluent thus obtained to result in crystallization of said L- amino acid, and isolation said crystalline L- amino acid from said fermentation liquor.

4997817

P H Y L L A N T H O S T A T I N A

George R Pettit assigned to Arizona Board of Reagents

An unusal cytostatic (PS ED50 4 ug/ml) lignan ester has been isolated from the Central

M E T H O D F O R R E C O V E R I N G A P U R I F I E D A N I M A L G R O W T H

H O R M O N E O R P O L Y P E P T I D E A N A L O G T H E R E O F F R O M A

B A C T E R I A L C E L L

Haim Aviv, Marian Gorecki, Avigdor Levanon, Amos Oppenheim, Tikva Vogel, Elisha Zeelon, Menachem Zeevi, Rehovot, Israel assigned to Bio-Technology General Corp

A method is provided for recovering a purified animal growth hormone or a polypeptide analog thereof having substantially the same amino acid sequence as, and the biological activity of, the corresponding naturally-occurring animal growth hormone from a bacterial cell in which the animal growth hormone or polypeptide analog has been produced by means of expres- sion of a plasmid encoding the hormone or poly- peptide analog which comprises: (a) disrupting the cell wall of the bacterial cell in a buffered neutral pH solution so as to produce a lysate containing precipitated hormone or polypeptide analog; (b) recovering the resulting precipitated hormone or polypeptide analog; (c) suspending the precipitated hormone or polypeptide analog so recovered in distilled water; (d) treating the resulting precipitate-containing suspension with a sodium hydroxide solution having an alkaline pH of about 11.8 so as to solubilize the pre- cipitate and thus the hormone or polypeptide analog contained therein; (e) separating the solubilized hormone or polypeplide analog from other soluble components by gel filtration chromatography; and (0 subjecting the hormone