Resolution of the major hemorrhagic component of Trimeresurus flavoviridis venom into two parts

Omori-Satoh, Tamotsu; Sadahiro, Seiji

doi:10.1016/0005-2795(79)90151-x

Cited by 58 publications

(14 citation statements)

References 21 publications

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“…P-IIIc has been reported for HV1 from P. flavoviridis venom, VAP1 from C. atrox venom, VLAIPs from V. lebetina venom, and TSV-DM from P. stejnegeri venom, and most of these proteins were shown to induce apoptosis in vascular endothelial cells (Masuda et al, 2001(Masuda et al, , 2000(Masuda et al, , 1997Samel et al, 2012;Trummal et al, 2005;Wan et al, 2006). Many P-IIIc SVMPs, such as VAP1 (MHD: 8 mg) from C. atrox (Kikushima et al, 2008) and VaH3 (MHD: 10 mg) from Vipera ammodytes (Sajevic et al, 2013), exhibit weaker hemorrhagic activities than those of with P-IIIa/b SVMPs, such as atrolysin A (HTa) (MHD: 0.04 mg) from C. atrox (Bjarnason and Tu, 1978) and HR1B (MHD: 0.01 mg) from P. flavoviridis (Omori-Satoh and Sadahiro, 1979). In the present study, hemorrhagic activity was measured in a maximum amount of 1 mg. SV-PAD-2 may also show hemorrhagic activity at doses of 10 mg or more because the MHD of VAP1 and VaH3, belonging to class P-IIIc, were 8 mg and 10 mg, respectively.…”

Section: Discussionmentioning

confidence: 98%

Purification and characterization of two high molecular mass snake venom metalloproteinases (P-III SVMPs), named SV-PAD-2 and HR-Ele-1, from the venom of Protobothrops elegans (Sakishima-habu)

Oyama

Takahashi

2015

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Section: Discussionmentioning

confidence: 98%

Purification and characterization of two high molecular mass snake venom metalloproteinases (P-III SVMPs), named SV-PAD-2 and HR-Ele-1, from the venom of Protobothrops elegans (Sakishima-habu)

Oyama

Takahashi

2015

Toxicon

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“…A highly purified hemorrhagic principle (HR 1 B) was obtained as described previously (15). HR1B at 2 mg/ml was detoxified at 37 C at three different pH values.…”

Section: Methodsmentioning

confidence: 99%

EFFECTS OF pH AND LYSINE DURING DETOXIFICATION OF A HEMORRHAGIC PRINCIPLE OF HABU SNAKE (TRIMERESURUS FLAVOVIRIDIS) VENOM WITH FORMALIN ON THE IMMUNOGENICITY OF THE TOXOID

Sadahiro

Omori-Satoh

Kondo

et al. 1984

JJMSB

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SUMMARY: A hemorrhagic principle (HR 1 B) isolated from the venom of Habu snake (Trimeresurus flavoviridis) was detoxified with formalin at pH 5, 7 and 9. Higher pH shortened the period needed for detoxification and lowered the final formalin concentration required for complete detoxification. The extent of polymerization and the immunogenicity of the toxoid formed were dependent upon pH during detoxification; the lower the pH, the higher the extent of polymerization and the immunogenicity of the toxoid. The higher immunogenicity possessed by the toxoid with higher extent of polymerization was confirmed by fractionation of the toxoid prepared at pH 7 on Sephadex G-200 and by comparing the immunogenicity of the toxoid fractions . The presence of lysine during detoxification brought about a partially polymerized toxoid having new immunogenic characteristics and a higher immunogenicity.

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“…Several SVMPs, HSF, and 5 hSSPs were prepared as previously described. 18,23,[26][27][28] The serum was fractionated by cold ethanol precipitation 7) with 0.5, 0.75, 1.25, and 2.0 volumes of ethanol, respectively, yielding E 0.5 , E 0.75 , E 1.25 , and E 2.0 . NBromosuccinimide (NBS), thermolysin, 2,4,6-trinitrobenzenesulphonic acid (TNBS), and trypsin were purchased from Sigma Chemical Co. (St. Louis, MO, USA).…”

Section: Materials and Animalsmentioning

confidence: 99%

Structural analysis and characterization of new small serum proteins from the serum of a venomous snake (Gloydius blomhoffii)

Shioi

Deshimaru

Terada

2014

Bioscience, Biotechnology, and Biochemistry

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Some snakes have several anti-toxic proteins in their sera that neutralize their own venom. Five new small serum proteins (SSPs) were isolated from Japanese mamushi (Gloydius blomhoffii) serum by gel-filtration and RP-HPLC, and their N-Terminal sequences were determined. The amino acid sequences of the precursor proteins were deduced from the nucleotide sequences of cDNAs encoding them. Due to the sequence similarity to those of SSPs in habu snake (Protobothrops flavoviridis) serum (>75% identity), these proteins were designated mSSP-1 to mSSP-5 as the homologs of habu proteins. mSSP-1 was stable at 100 °C and in the pH range of 1–10, and inhibited the proteolytic activity of a certain snake venom metalloproteinase. The inhibitory activity was extinguished by modifying the amino groups of mSSP-1. mSSP-1 is the first prostate secretory protein of the 94 amino acid-family protein with a carbohydrate chain in the Asn37 residue.

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Resolution of the major hemorrhagic component of Trimeresurus flavoviridis venom into two parts

Cited by 58 publications

References 21 publications

Purification and characterization of two high molecular mass snake venom metalloproteinases (P-III SVMPs), named SV-PAD-2 and HR-Ele-1, from the venom of Protobothrops elegans (Sakishima-habu)

Purification and characterization of two high molecular mass snake venom metalloproteinases (P-III SVMPs), named SV-PAD-2 and HR-Ele-1, from the venom of Protobothrops elegans (Sakishima-habu)

EFFECTS OF pH AND LYSINE DURING DETOXIFICATION OF A HEMORRHAGIC PRINCIPLE OF HABU SNAKE (TRIMERESURUS FLAVOVIRIDIS) VENOM WITH FORMALIN ON THE IMMUNOGENICITY OF THE TOXOID

Structural analysis and characterization of new small serum proteins from the serum of a venomous snake (Gloydius blomhoffii)

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