Complete amino acid sequences of two protease inhibitors in the venom of Bungarus fasciatus

Abstract

Two analogous protease inhibitors, VIIIb and IX in the venom of Bungarus fasciatus were reduced and carboxymethylated. Tryptic peptides were separated by cellulose thin‐layer peptide mapping technique, and amino acid sequences were analyzed by DABITC/PITC double coupling method. Alignment of all tryptic peptides was established by analyses of chymotryptic peptides and further confirmed by Staphylococcus aureus V8 protease digestion. IX consisted of 65 amino acid residues. VIIIb consisted of 62 residues, identical to the N‐terminal 62‐amino acid sequence of IX.

Purification, characterization and molecular cloning of chymotrypsin inhibitor peptides from the venom of Burmese Daboia russelii siamensis

“…A typical trypsin inhibitor has a positively charged Arg or Lys residue at P 1 , whereas a chymotrypsin inhibitor has a large hydophobic Phe, Leu, Met, Tyr, or Trp residue [23]. Two chymotrypsin inhibitors containing Asn at P 1 were also found in Bungarus fasciatus venom [25] and Ophiophagus hannah venom [3]. In this study the P 1 amino acid residue of BBPTI-1 and BBPTI-5 is leucine (Fig.…”

“…To date a number of BPTI-like superfamily serine protease inhibitors from Viperidae and Elapidae venoms have been purified or characterized [3,4,12,13,15,16,18,19,25,26,[29][30][31][32][33][34]35,36,39]. In this paper, one chymotrypsin inhibitor, BBPTI-1, was purified to homogeneity from the venom of Burmese Daboia russelli siamensis by gel filtration, cation exchange and reversed phase chromatography.…”

Protease Inhibitors from Marine Venomous Animals and Their Counterparts in Terrestrial Venomous Animals

“…Until now, two PIs have been isolated from Bungarus fasciatus venom [54,55]. The first of them was denoted protease inhibitor IX (or BF9, Table 1) and consists of a polypeptide chain of 65 amino acid residues that, when cleaved, generates the protease inhibitor VIIIb [54].…”

“…The first of them was denoted protease inhibitor IX (or BF9, Table 1) and consists of a polypeptide chain of 65 amino acid residues that, when cleaved, generates the protease inhibitor VIIIb [54]. BF9 specifically inhibits α-chymotrypsin in a 1:1 molar ratio and is structurally similar to the Kunitz-type toxins [54,118]. The second is a Kunitz-type serine protease inhibitor named bungaruskunin (Table 1), which was characterized from venom and also cloned from venom glands [55].…”

Análise do transcriptoma do fígado da serpente Bothrops jararaca utilizando expressed sequences tags (ESTs).

“…Inibidores de serinoproteases foram isolados dos venenos de serpentes da família Viperidae e Elapidae (FILIPPOVICH et al, 2002;GUO et al, 2001;WU;LO, 1983;LI;GREENAWAY, 2006;RITONJA;TURK;GUBENSEK, 1983;ZAIDI;JÖRNVALL, 1990a;SHAFQAT et al, 1990b;SCHWEITZ et al, 1994) os quais são em grande parte inibidores de serinoproteases pertencentes à família de inibidores de tripsina pancreática bovina tipo Kunitz (BPTI) (CHENG et al, 2012;LASKOWSKI, 1986;LASKOWSKI;KATO, 1980 O estudo de inibidores de proteases no plasma de serpentes pode levar ao desenvolvimento de novas alternativas terapêuticas para uma variedade de doenças (DE MORAIS et al, 2009;EARL et al, 2012;OLIVEIRA et al, 2008;OLIVEIRA et al, 2011;SANTOS-FILHO et al, 2011;SOARES et al, 2003;ZHANG et al, 2001;ZHANG et al, 2007). Portanto, faz-se necessário a identificação de moléculas do fígado para entender o processo de inibição de toxinas por proteínas do plasma de B. jararaca.…”