Polydispersity of Serratia marcescens nuclease at optimum pH

M. N. Filimonova; M. J. Benedik; N. G. Urazov; I. B. Leshchinskaya

Polydispersity of Serratia marcescens nuclease at optimum pH

M. N. Filimonova^*, M. J. Benedik, N. G. Urazov, I. B. Leshchinskaya

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

3 Citations (Scopus)

Abstract

Treatment with dimethyl suberimidate, a cross-linking bifunctional agent, showed that Sm1 and Sm2 nucleases of Serratia marcescens B10M1 are polydisperse in solution and consist of monomers and dimers at the level of pH optimal for the enzyme activity. The data suggest that nucleases from the strain B10M1 and any other strain are polydisperse at pH optimum if their amino acid sequences are identical.

Original language	English
Pages (from-to)	17-20
Number of pages	4
Journal	Applied Biochemistry and Microbiology
Volume	35
Issue number	1
Publication status	Published - Jan 1999
Externally published	Yes

Cite this

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title = "Polydispersity of Serratia marcescens nuclease at optimum pH",

abstract = "Treatment with dimethyl suberimidate, a cross-linking bifunctional agent, showed that Sm1 and Sm2 nucleases of Serratia marcescens B10M1 are polydisperse in solution and consist of monomers and dimers at the level of pH optimal for the enzyme activity. The data suggest that nucleases from the strain B10M1 and any other strain are polydisperse at pH optimum if their amino acid sequences are identical.",

author = "Filimonova, {M. N.} and Benedik, {M. J.} and Urazov, {N. G.} and Leshchinskaya, {I. B.}",

year = "1999",

month = jan,

language = "English",

volume = "35",

pages = "17--20",

journal = "Applied Biochemistry and Microbiology",

issn = "0003-6838",

publisher = "Pleiades Publishing",

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T1 - Polydispersity of Serratia marcescens nuclease at optimum pH

AU - Filimonova, M. N.

AU - Benedik, M. J.

AU - Urazov, N. G.

AU - Leshchinskaya, I. B.

PY - 1999/1

Y1 - 1999/1

N2 - Treatment with dimethyl suberimidate, a cross-linking bifunctional agent, showed that Sm1 and Sm2 nucleases of Serratia marcescens B10M1 are polydisperse in solution and consist of monomers and dimers at the level of pH optimal for the enzyme activity. The data suggest that nucleases from the strain B10M1 and any other strain are polydisperse at pH optimum if their amino acid sequences are identical.

AB - Treatment with dimethyl suberimidate, a cross-linking bifunctional agent, showed that Sm1 and Sm2 nucleases of Serratia marcescens B10M1 are polydisperse in solution and consist of monomers and dimers at the level of pH optimal for the enzyme activity. The data suggest that nucleases from the strain B10M1 and any other strain are polydisperse at pH optimum if their amino acid sequences are identical.

UR - http://www.scopus.com/inward/record.url?scp=0032621891&partnerID=8YFLogxK

M3 - Article

AN - SCOPUS:0032621891

SN - 0003-6838

VL - 35

SP - 17

EP - 20

JO - Applied Biochemistry and Microbiology

JF - Applied Biochemistry and Microbiology

IS - 1

ER -

Polydispersity of Serratia marcescens nuclease at optimum pH

Abstract

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