5585462 Cloning of perilipin proteins

5585462 Cloning of perilipin proteins

Biotochnology Advances, Vol. 15, Nos. 3/4, pp. 659-807, 1997 Copyright © 1997 Elsevier Science Inc. Printed in the USA. All rights reserved 073,*-9750...

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Biotochnology Advances, Vol. 15, Nos. 3/4, pp. 659-807, 1997 Copyright © 1997 Elsevier Science Inc. Printed in the USA. All rights reserved 073,*-9750/97 $32.00 + .00

NEW PATENTS

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This section eontaim abstracts and, where appropriate, illustr~tiotm of reconfly issued United States patents and publi~ed patent application filed from over 30 countries under the Patent Coopcaation Treaty. This information was obtained from recant additions to the PATSEARCH® online database in accordance with intea'estlxafide* developed by the Editom. Further Lnfon'aationabout online patent searching can be obtained from Research on Demand, Inc., 2421 Fourth Street, Ste. C., Berkeley, CA 94710, U.S.A. [Tel. 510-841-1145; Fax 510-841-6331.]

Mutation/Genetic En~neering Techniques 5585462 CLONING

the construction of a gene-targeting vector to produce animals deficient in D4 through disruption of the gene by homologous recombination. These animals can then be used as models for fundamental and applied research on the GTP-binding proteins.

OF PERILIPIN

PROTEINS Londos Constantine; Greenberg Andrew S; Kimmel Alan R; Egan John Garrett Park, MD, UNITED STATES Assigned to United States of America

5585542 DNA SEQUENCES ENCODING AT LEAST PART OF THE

The present invention provides isolated nucleic acid sequences, i.e., polynucleotides, which encode a family of perilipin proteins. The present invention also provides isolated, substantially purified perilipin proteins which are useful as markers for differentiating true adipocytes from non-adipocyte cells which, as a result of pathophysiological conditions, assume adipocyte characteristics and become lipid-laden. The present invention further provides methods for producing a substantially purified perilipin protein and methods for detecting the presence of such perilipin proteins in a biological samples.

TOMATO ENZYME ENDOPOLYGALACTURONASE PG1 BETA-SUBUNIT Brady Colin; Lee Elizabeth; Pogson Barry J; Orr Glenda; Speirs Jame Sydney, AUSTRALIA Assigned to Commonwealth Scientific and Industrial Research Organisation PCT No. PCT/AU91/O0594 Sec. 371 Date Oct. 25, 1993 Sec. 102(e) Date Oct. 25, 1993 PCT Filed Dec. 20, 1991 PCT Pub. No. WO92/11374 PCT Pub. Date Jul. 9, 1992. The present invention provides an isolated DNA sequence which encodes at least partof the tomato enzyme endopolygalacturonase PGI beta-subunit. This DNA sequence preferably encodes a polypeptide, the N-terminal amino acid sequence of which is: E-K-H-S-G-D-I-H. In other preferred forms of the invention the DNA sequence encodes a polypeptide which includes one of the following amino acid sequences: E-K-H-S -G or N-Y-G-Q-X-F-N-E-G. The DNA sequence of the present invention may be used to produce genetically engineered tomato plants with modified ripening characteristics.

5585478 D4 GENE

AND METHODS

OF

USE THEREOF Lim Bing; Lelias Jean-Michel; Adra Chaker N; Ko Jone Dorchester, MA, UNITED STATES Assigned to Beth Israel Hospital Association The sequence, molecular structure and expression of a cDNA clone, denoted D4, of human and murine origin, preferentially expressed in hematopoietic cells is described herein. The human cDNA clone has been expressed in bacteria and the predicted 24 Kd protein purified. The protein has been used in studies of its biochemical function. As predicted on the basis of sequence, D4 can function as a GDP-dissociation inhibitor of at least several small GTP-binding proteins (CDC42 and rac). The D4 protein was used to generate a polyclonal antibody specifm for the protein. The human cDNA was used to obtain several full length murine genomic clones. A clone has been analyzed and sequenced to use for

5585543 ALTERATION OF PLANT SELF-COMPATIBILITY USING GENETIC MANIPULATION OF THE S-GENES Kao Teh-hui State College, PA, UNITED STATES Assigned to The Penn State Research Foundation 659