Policy change implications for forest water protection in Sweden over the last 50 years.

Improving water quality has become an important environmental issue, spurred in part by the Water Framework Directive. However, the relationship of policy change with forest water protection measures is relatively unknown. We analyzed how policy and practice have developed in Sweden using 50 years of historic data from the Krycklan Catchment Study, focusing on riparian buffers.

Spectroscopic properties and stability of the neurotoxic complex. Vipoxin and its components.

The neurotoxin Vipoxin from the venom of Vipera ammodytes meridionalis is a complex between a toxic basic phospholipase A2 (PLA2) and a non-toxic acidic protein inhibitor (Inh). Tryptophan fluorescence parameters are determined for the complex and for its components. Iodide, caesium and acrylamide are not efficient quenchers of the Vipoxin indole emission.

Crystal structure of vipoxin at 2.0 A: an example of regulation of a toxic function generated by molecular evolution.

Vipoxin is the main toxic component in the venom of the Bulgarian snake Vipera ammodytes meridionalis, the most toxic snake in Europe. Vipoxin is a complex between a toxic phospholipase A2 (PLA2) and a non-toxic protein inhibitor. The structure is of genetic interest due to the high degree of sequence homology (62%) between the two functionally different components.

Crystallization and preliminary X-ray analysis of vipoxin, a complex between a toxic phospholipase A2 and its natural polypeptide inhibitor.

The toxin vipoxin, which is a complex between a basic toxic phospholipase A2 and an acidic non-toxic protein inhibitor, is found in the venom of the Bulgarian viper (Vipera ammodytes ammodytes), the most toxic snake in Europe. The two polypeptide chains each consist of 122 residues and are highly homologous (62%). The vipoxin complex is the first reported example of a high degree of structural homology between an enzyme and its natural inhibitor.

Crystals of phospholipase A2 inhibitor. The non-toxic component of vipoxin from the venom of Bulgarian viper (Vipera ammodytes).

Phospholipase A2 inhibitor, the non-toxic, acidic component of vipoxin from the venom of Bulgarian viper (Vipera ammodytes), has been crystallized. The tetragonal crystals obtained, exhibit the symmetry of space group P4(1)22 (or 4(3)22) with unit cell dimensions a = b = 59.9 A; c = 141.

Biological tests for opiate activity of newly-synthesized compounds--opioid peptides and cyclic beta-diketones.

A group of newly-synthesized (Leu5) enkephalinamides and their derivatives, with incorporated D-amino acids, as well as a group of cyclic beta-diketones from the group of 1, 3-indandiones, were partially pharmacologically characterized in experiments in vivo and in vitro. The substances studied, applied subcutaneously in doses of 50 to 1250 micrograms/kg bogy mass in mice, did not induce symptoms of acute and late toxicity. According to the parameters of the neuropharmacological screening tests performed, no significant differences were observed between the mice treated with the agents tested and the control mice.

Sequence homology between phospholipase and its inhibitor in snake venom. The primary structure of phospholipase A2 of vipoxin from the venom of the Bulgarian viper (Vipera ammodytes ammodytes, Serpentes).

The amino-acid sequence of phospholipase A2 from the neurotoxin vipoxin of the Bulgarian Viper (Vipera ammodytes ammodytes, Serpentes) is presented. The enzyme consists of 122 amino-acid residues including 7 disulfide bonds and thus belongs to phospholipases A2 group IIA. The sequence was determined by automatic Edman degradation of the intact chain and of the peptides obtained after tryptic hydrolysis of the oxidized chain.

Sequence homology between phospholipase and its inhibitor in snake venom. The primary structure of the inhibitor of vipoxin from the venom of the Bulgarian viper (Vipera ammodytes ammodytes, Serpentes).

We are presenting the first primary structure of a snake venom inhibitor. It was isolated from the neurotoxin vipoxin of the Bulgarian Viper (Vipera ammodytes ammodytes, Serpentes) which represents a complex of a strong toxic basic protein with phospholipase A2 activity (2 isoenzymes) and the nontoxic acidic component functioning as its inhibitor. The sequence was established by automatic degradation in a liquid phase sequenator on the S-carboxymethylated chain and on the peptides obtained by tryptic hydrolysis of the oxidized chain.

Pyridoxal phosphate modified cytochromes c. Identification and electron transfer properties.

The preparation, purification and characterization of the three singly, three doubly and one triply substituted derivatives of cytochrome c modified by pyridoxal phosphate (PLP) at lysine residues are reported. The PLP positions in PLP derivatives were determined by the amino acid analysis and sequence of PLP peptides. The results identified the lysine at position 86 in one of the singly substituted, lysine 79 in the other singly substituted and lysines 86 and 79 in the third doubly substituted cytochrome c derivatives.