L. L. Zavalova
Current Organizations / Institutes
The organizations/institutes from the scholar's latest article
Previous Organizations / Institutes
The organizations / institutes from the scholar's other articles in the past ten years
Research Subjects
L. L. Zavalova has a total of 31 co-authors. Here are the top co-authors by number of shared publications:
I. P. Baskova
Lomonosov Moscow State University
3 shared publicationsL. L. Zavalova
Russian Academy of Sciences
3 shared publicationsA. V. Basanova
Lomonosov Moscow State University
2 shared publicationsA V Basanova
1 shared publicationA. V. Sass
Russian Academy of Sciences
1 shared publicationA.A Tagaev
Shemyakin and Ovchinnikov Institute of Bioorganic Chemistry, 117997 Moscow, Russian Federation
1 shared publication
Latest Publications
- 1 July 2004
- Published by Springer Nature in Biochemistry (Moscow)
- Vol. 69 (7) , 776-781
Recombinant Destabilase-Lysozyme: Synthesis de novo in E. coli and Action Mechanism of the Enzyme Expressed in Spodoptera frugiperda
Destabilase-lysozyme (DL) from salivary gland secretion of the medicinal leech ( Hirudo medicinalis) is as a member of the invertebrate lysozyme family, which sharply differs from other lysozyme...
- 1 July 2004
- Published by Springer Nature in Biochemistry (Moscow)
- Vol. 69 (7) , 776-781
Recombinant Destabilase-Lysozyme: Synthesis de novo in E. coli and Action Mechanism of the Enzyme Expressed in Spodoptera frugiperda
Destabilase-lysozyme (DL) from salivary gland secretion of the medicinal leech ( Hirudo medicinalis) is as a member of the invertebrate lysozyme family, which sharply differs from other lysozyme...
- 23 May 2003
- Published by Elsevier in Biochemical and Biophysical Research Communications
- Vol. 306 (1) , 318-323
Multiple forms of medicinal leech destabilase-lysozyme
- 23 May 2003
- Published by Elsevier in Biochemical and Biophysical Research Communications
- Vol. 306 (1) , 318-323
Multiple forms of medicinal leech destabilase-lysozyme
- 1 January 2002
- Published by Springer Nature in Biochemistry (Moscow)
- Vol. 67 (1) , 143-150
Vascular–Platelet and Plasma Hemostasis Regulators from Bloodsucking Animals
Saliva of bloodsuckers (leeches, insects, ticks, vampire bats) contains various regulators of some hemostatic stages. This review summarizes information on their structural characteristics and...
- 1 January 2002
- Published by Springer Nature in Biochemistry (Moscow)
- Vol. 67 (1) , 143-150
Vascular–Platelet and Plasma Hemostasis Regulators from Bloodsucking Animals
Saliva of bloodsuckers (leeches, insects, ticks, vampire bats) contains various regulators of some hemostatic stages. This review summarizes information on their structural characteristics and...
- 1 January 2002
- Published by Springer Nature in Biochemistry (Moscow)
- Vol. 67 (1) , 135-142
Fibrinogen–Fibrin System Regulators from Bloodsuckers
Thrombin inhibitors from bloodsucking leeches and insects that block conversion of fibrinogen to fibrin are considered. Regulatory mechanisms influencing the fibrinogen–fibrin system in leeches...
- 1 January 2002
- Published by Springer Nature in Biochemistry (Moscow)
- Vol. 67 (1) , 135-142
Fibrinogen–Fibrin System Regulators from Bloodsuckers
Thrombin inhibitors from bloodsucking leeches and insects that block conversion of fibrinogen to fibrin are considered. Regulatory mechanisms influencing the fibrinogen–fibrin system in leeches...
- 1 December 2001
- Published by Springer Nature in Biochemistry (Moscow)
- Vol. 66 (12) , 1368-1373
Separation of Monomerizing and Lysozyme Activities of Destabilase from Medicinal Leech Salivary Gland Secretion
Destabilase, endo-ε-(γ-Glu)-Lys-isopeptidase, was prepared from the salivary gland secretion of the medicinal leech ( Hirudo medicinalis). The secretion prepared by the known method of Rigbi et al....
- 1 December 2001
- Published by Springer Nature in Biochemistry (Moscow)
- Vol. 66 (12) , 1368-1373
Separation of Monomerizing and Lysozyme Activities of Destabilase from Medicinal Leech Salivary Gland Secretion
Destabilase, endo-ε-(γ-Glu)-Lys-isopeptidase, was prepared from the salivary gland secretion of the medicinal leech ( Hirudo medicinalis). The secretion prepared by the known method of Rigbi et al....
- 1 July 2001
- Published by Springer Nature in Biochemistry (Moscow)
- Vol. 66 (7) , 703-714
Proteinase Inhibitors from the Medicinal Leech Hirudo medicinalis
The medicinal leech Hirudo medicinalisproduces various types of proteinase inhibitors: bdellins (inhibitors of trypsin, plasmin, and acrosin), hirustasin (inhibitor of tissue kallikrein, trypsin,...
- 1 July 2001
- Published by Springer Nature in Biochemistry (Moscow)
- Vol. 66 (7) , 703-714
Proteinase Inhibitors from the Medicinal Leech Hirudo medicinalis
The medicinal leech Hirudo medicinalisproduces various types of proteinase inhibitors: bdellins (inhibitors of trypsin, plasmin, and acrosin), hirustasin (inhibitor of tissue kallikrein, trypsin,...
- 1 March 2000
- Published by Elsevier in Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
- Vol. 1478 (1) , 69-77
Destabilase from the medicinal leech is a representative of a novel family of lysozymes
- 1 March 2000
- Published by Elsevier in Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
- Vol. 1478 (1) , 69-77
Destabilase from the medicinal leech is a representative of a novel family of lysozymes
- 1 June 1999
- Vol. 25 (6) , 435-8
[The hydrolysis of Glu(gamma-epsilon)Lys-amide bonds in D-dimer fragment of fibrin by destabilase from medicinal leech].
A study was made of the dependence of the hydrolysis rate of isopeptide bonds in the D-dimer, the product of limited proteolysis of the stabilized fibrin by plasmin, on the high-molecular substrate concentration catalyzed by destabilase from the medicinal leech. The formation of the reaction product was electrophoretically measured by the increase in the quantity of D-monomer. This dependence was shown to be nonlinear.
- 1 June 1999
- Vol. 25 (6) , 435-8
[The hydrolysis of Glu(gamma-epsilon)Lys-amide bonds in D-dimer fragment of fibrin by destabilase from medicinal leech].
A study was made of the dependence of the hydrolysis rate of isopeptide bonds in the D-dimer, the product of limited proteolysis of the stabilized fibrin by plasmin, on the high-molecular substrate concentration catalyzed by destabilase from the medicinal leech. The formation of the reaction product was electrophoretically measured by the increase in the quantity of D-monomer. This dependence was shown to be nonlinear.