Purification et propriétés physico-chimiques, chimiques et biologiques d'une phospholipase A2...

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Kovooa, J. and Zrt .sata0eo, L . (I-ab. dévolution des Etter organisés et Lab, ed Microscopie électronique appliqué ~ Ia Biologie (C.N.R.S.), IOS, boulevard Raspad, F 75006 Paris, France) . Histok~e et inftastructrtre de la glande dxlicerieane de Scytoda deliQatrrla Sim. (~4rarteidae, Scytodidae). Anno~r Sel. nat. 14, 333, 1972 . Try c~ucEw~t gland of Scytodu del/catula Sim . contains five setxetory parts, which aeaete throe products, Lobe I is ~ericigenous' and contains a rostra) islet of cells which are rich in proteins and acid tntrcosubstanoea . Lobes II and Ill produce substances 'giving the imptesaion' that they arc toetic. The functional role of the lobe IV is not clear. The intracheliceral portion of the gland (cancer cants to be involved in some regulation . F .E .R . SAEtnvcEx, C. B. and ütcestvaorttAt~t, R. D. (Departaxnt of Microbiology, Health Sciences Crnter, Louisville, Krntucky, U .S .A .) . Hypersensitivity responses to ber venom and to rnelittin . lnt, Arclrs. Allergy oppl. lnrrnnn. 46, 28, 1974. BEE VENOM iS both antigenic and anaphylactoid in that it releases histamine and causes degranulation of mast cells. In this study, mice sensitized with venom showed both cutaneous and systemic hypersensitivity on challenge. This was enhanced by adrcnakctomy or heat stress . Cutarteous sensitivity could be passively traruferrcd . All immune and anaphylactoid responses to ba venom were reproduced with rmllitin, suggest- ing that this polypcptidc is an important allergen as well as the trta~jor toxic component of ba venom . Immunization enhanced systemic reactions to phospholipase A but did not affect skin reactions . S.A .M . DELURt, P. J . (Institut Pasteur, Service de Recherches sur les Venins, 9238Q-Garches, France). Purification et propriétés physico-chimiques, chimiques et biologiques d'une phospholipase A2 to~iquc isolée d'un venin de serpent Vipcridac : Vlpera berrrs. 8loclrimit 35, 1031, 1973 . TFIL4 PAPER dcccriba the isolation from Vipers berus venom of a toxic phospholipase A2, using ion exchange chromatography and gel filtration . The purified enzyme (P4) was found to be fairly homogeneous by physico- chcmit~l criteria (chromatography, electrophorcais and immuno~kctrophorais), as well as chcmiutl tats (amino acid composition, determination of N- and C-terminal amino acids). The amino acid composition of this basic protein (pHi s 9) shows sonic similarities with those of two other phospholipasa A2 isolated from the same venom (fractions PI and P2) aced with those of other phospholipases A2 found in other snake venorrts. Flowcver, that molecules an: generally more acidic and non toxic . P4 was shown to be anti- grnically difTcrcnt From the other phospholipases present in the same venom . F .E.R . PECK, M. L. et ol . Procaminc and other basic peptides in the venom of the honeybee (ApLr rrrrllijera). J . agrle . Fd. Clunr. 22, 51, 1974. THE PAYER has been presented at a symposium . Most of it reviews some basic facts about ba venom . The last part deals with procesmine . According to unpublished work of the authors, ba venom contains two pcptida having a histamine residue at their Gterminus : Ales-0ly-Pro-Gln-Histamine Ala-Gly-Gln-Gly-Histamine . The latter peptide has ban synthesized by combination of Nam-benzylhistamine with N-benzyloxycarbonyl- t .-glutaminyl glycine, removal of the N-benzyloegrcarbonyl group with HBr in acetic acid, coupling with N-bertzyloxycarbonyl-[ .-alanylglycine via the mixed anhydride method, and ttrattrtent with sodium in liquid ammonia . The product was purißed by column chromatography and found to be identical with the natural peptide . No biological data arc mentioned . Horcrrr , R . et al, Acute allergic systemic reaction to ba and wasp stings : rrsulta and duration of specific hyposensitization, etc . Sehwels. rued. Wuhr. 104, 221, 1974. ACCORDtNCi to the observations of the authors and findings from the literature, about 40 per ant of the case historic of anaphylactic shocks due to insect stings imply respiratory manifestations (edema in the upper respiratory tract, bronchial obstruction, acute pulmonary edema). The respiratory form appears to TOXICON 1971 r ól. 11 E.H .

Transcript of Purification et propriétés physico-chimiques, chimiques et biologiques d'une phospholipase A2...

Page 1: Purification et propriétés physico-chimiques, chimiques et biologiques d'une phospholipase A2 toxique isolée d'un venin de serpent Viperidae: Vipera berus: Delori, P. J. (Institut

Kovooa, J. and Zrt.sata0eo, L. (I-ab. dévolution des Etter organisés et Lab, ed Microscopieélectronique appliqué ~ Ia Biologie (C.N.R.S.), IOS, boulevard Raspad, F 75006 Paris, France).Histok~e et inftastructrtre de la glande dxlicerieane de Scytoda deliQatrrla Sim. (~4rarteidae,

Scytodidae). Anno~r Sel. nat. 14, 333, 1972.

Try c~ucEw~t gland of Scytodudel/catula Sim. contains five setxetory parts, which aeaete throe products,Lobe I is ~ericigenous' and containsa rostra)isletofcells which arerich in proteinsand acid tntrcosubstanoea .Lobes II and Ill produce substances 'giving the imptesaion' that they arc toetic. The functional role of thelobe IV is not clear. The intracheliceral portion ofthe gland (cancer cants to be involved in some regulation.

F.E.R .

SAEtnvcEx, C. B. and ütcestvaorttAt~t, R. D. (Departaxnt of Microbiology, Health SciencesCrnter, Louisville, Krntucky, U.S.A .) . Hypersensitivity responses to ber venom and to rnelittin .

lnt, Arclrs. Allergy oppl. lnrrnnn. 46, 28, 1974.

BEE VENOM iS both antigenic and anaphylactoid in that it releases histamine and causes degranulation ofmast cells. In this study, mice sensitized with venom showed both cutaneous and systemic hypersensitivityon challenge. This was enhanced by adrcnakctomy or heat stress . Cutarteous sensitivity could be passivelytraruferrcd . All immune and anaphylactoid responses to ba venom were reproduced with rmllitin, suggest-ing that this polypcptidc is an important allergen as well as the trta~jor toxic component of ba venom.Immunization enhanced systemic reactions to phospholipase A but did not affect skin reactions .

S.A.M .

DELURt, P. J . (Institut Pasteur, Service de Recherches sur les Venins, 9238Q-Garches, France).Purification et propriétés physico-chimiques, chimiques et biologiques d'une phospholipase A2

to~iquc isolée d'un venin de serpent Vipcridac: Vlpera berrrs. 8loclrimit 35, 1031, 1973 .

TFIL4 PAPER dcccriba the isolation from Vipers berus venom of a toxic phospholipase A2, using ionexchangechromatography and gel filtration . The purified enzyme (P4) was found to be fairly homogeneous by physico-chcmit~l criteria (chromatography, electrophorcais and immuno~kctrophorais), as well as chcmiutl tats(amino acid composition, determination of N- and C-terminal amino acids). The amino acid compositionof this basic protein (pHi s 9) shows sonic similarities with those of two other phospholipasa A2 isolatedfrom the same venom (fractions PI and P2) aced with those of other phospholipases A2 found in othersnakevenorrts. Flowcver, that molecules an: generally more acidic and non toxic. P4 was shown to be anti-grnically difTcrcnt From the other phospholipases present in the same venom.

F.E.R .

PECK,M. L. et ol . Procaminc and other basic peptides in the venom of the honeybee (ApLr rrrrllijera).J.agrle . Fd. Clunr. 22, 51, 1974.

THE PAYER has been presented at a symposium. Most of it reviews some basic facts about ba venom. Thelast part deals with procesmine. According to unpublished work of the authors, ba venom contains twopcptida having a histamine residue at their Gterminus:

Ales-0ly-Pro-Gln-HistamineAla-Gly-Gln-Gly-Histamine .

The latter peptide has ban synthesized by combination of Nam-benzylhistamine with N-benzyloxycarbonyl-t.-glutaminyl glycine, removal of the N-benzyloegrcarbonyl group with HBr in acetic acid, coupling withN-bertzyloxycarbonyl-[.-alanylglycine via the mixed anhydride method, and ttrattrtent with sodium inliquid ammonia. The product was purißed by column chromatography and found to be identical with thenatural peptide . No biological data arc mentioned.

Horcrrr , R. et al, Acute allergic systemic reaction to ba and wasp stings : rrsulta and duration ofspecific hyposensitization, etc . Sehwels. rued. Wuhr. 104, 221, 1974.

ACCORDtNCi to the observations of the authors and findings from the literature, about 40 per ant of thecase historic of anaphylactic shocks due to insect stings imply respiratory manifestations (edema in theupper respiratory tract, bronchial obstruction, acute pulmonary edema). The respiratory form appears to

TOXICON 1971 ról. 11

E.H .