[The resistance of the DNA of cyanophage LPP-3 to the action of different restriction endonucleases]

Autor: M I, Mendzhul, S A, Syrchin, B A, Rebentish, A A, Averkiev, I V, Busakhina

Publikováno v: Mikrobiolohichnyi zhurnal (Kiev, Ukraine : 1993). 55(4)

Data on the study of structure peculiarities of cyanophage LPP-3 DNA are presented in the work. The length of cyanophage DNA calculated by means of the enzymatic hydrolysis by restrictases is 40 +/- 3.5 thou. pairs of bases. Cyanophage LPP-3 DNA was

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::f11953cdc52ffc94f423d38800c87246
https://pubmed.ncbi.nlm.nih.gov/8220827

[Features of genome expression of phage transposon D3112 of Pseudomonas aeruginosa in Escherichia coli bacteria: dependence of bacterial phenotype on copy number of D3112 genome]

Autor: M A, Trenina, V Z, Akhverdian, L G, Kolibaba, B A, Rebentish, V N, Krylov

Publikováno v: Genetika. 27(8)

Escherichia coli (RP4 :: D3112) bacteria manifest Tcs phenotype (thirty centigrade sensitivity), i.e. the cells do not divide and form colonies under conditions of lowered temperature (30 degrees C and lower), while cells grow normally at 42 degrees

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::36c37be7817116104b1afe53ad4d6a05
https://pubmed.ncbi.nlm.nih.gov/1662179

[A new site-specific endodeoxyribonuclease EcoHI]

Autor: L I, Glatman, A A, Terekhov, K V, Kalnin, A P, Bolotin, B A, Rebentish

Publikováno v: Molekuliarnaia genetika, mikrobiologiia i virusologiia. (3)

A new sitespecific endonuclease of the II class EcoHI has been isolated from Escherichia coli strain and characterized. Restriction endonuclease EcoHI recognises the nucleotide sequence C C (C/G) G G with the cleavage site between the fourth and fift

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::970a7293c955f153dd80adffd13819e9
https://pubmed.ncbi.nlm.nih.gov/2194120

Patents and literature

Autor: A, Rembaum, R P, Rohrbach, S, Klose, H G, Batz, M, Stoltz, A, Hagen, G, Weimann, S G, Wildman, P, Kwanyuen, G, Franzmann, H L, Wulsmann, T, Nakanishi, Y, Shigemasa, R, Monsheimer, E, Pfleiderer, T, Yoshioka, K, Teramoto, M, Shimamura, C K, Lee, M, Tamuri, M, Kanno, Y, Ishi, I, Kaetsu, M, Kumakura, M, Yoshida, G A, Strobel, D E, Johnson, V R, Srinivasan, Y C, Choi, H, Fukuda, T, Shiotani, W, Okada, R A, Messing, R A, Oppermann, L B, Simpson, M M, Takeguchi, M, Bigazzi, T B, Higerd, J M, Goust, W R, Tolbert, M J, Kuo, J, Feder, R N, Patel, C T, Hou, A I, Laskin, H, Yukawa, K, Osumi, Y, Takayama, A, Fujiwara, S, Masuda, F, Takaku, K, Ogasa, M, Kuboyama, M, Saito, N, Yanai, M, Nishida, O, Tosaka, E, Ono, M, Ishihara, H, Morioka, K, Takinami, A, Taoka, S, Uchida, J, Puls, M, Sinner, H H, Dietrichs, D T, Wicklow, R W, Detroy, R E, Heady, T, Nara, E, Knight, G T, Tsao, M R, Ladisch, C M, Ladisch, T A, Hsu, H J, Friesen, S, Pestka, J J, Manis, V G, Debabov, J I, Kozlov, N I, Zhdanova, E M, Khurges, N K, Yankovsky, M R, Rozinov, R S, Shakulov, B A, Rebentish, V A, Livshits, M M, Gusyatiner, S V, Mashko, V N, Moshentseva, L F, Kozyreva, R A, Arsatiants, H M, Goodman, J, Shine, P, Horst, D V, Goeddel, H L, Heyneker

Publikováno v: Applied Biochemistry and Biotechnology. 6:339-351

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a42c63149a4c90a450952c14f1395852
https://doi.org/10.1007/bf02798284

[Site-specific restriction endonuclease from a strain of Bacillus thuringiensis]

Autor: R R, Azizbekian, B A, Rebentish, T V, Stepanova, E M, Netyksa, M A, Bychkova

Publikováno v: Doklady Akademii nauk SSSR. 274(3)

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::9109e07d056d72ae70ccb8708062f9a8
https://pubmed.ncbi.nlm.nih.gov/6323119