Amino acid sequence of phospholipase A from porcine pancreas

1969 ◽  
Vol 188 (2) ◽  
pp. 351-352 ◽  
Author(s):  
S. Maroux ◽  
A. Puigserver ◽  
V. Dlouha ◽  
P. Desnuelle ◽  
G.H. De Haas ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Phospholipase A ◽  
Porcine Pancreas

The amino acid sequence of the phospholipase A2 isoenzyme from porcine pancreas

1979 ◽  
Vol 580 (2) ◽  
pp. 411-415 ◽  
Author(s):  
W.C. Puijk ◽  
H.M. Verheij ◽  
P. Wietzes ◽  
G.H. de Haas
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Phospholipase A2 ◽  
Porcine Pancreas

Amino Acid Sequence of Phospholipase A from Bungarus multicinctus Venom

1981 ◽  
Vol 89 (1) ◽  
pp. 37-47 ◽  
Author(s):  
Kiyoshi KONDO ◽  
Hiroko TODA ◽  
Kozo NARITA
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Phospholipase A

Characterization, amino acid sequence and evolution of edema-inducing, basic phospholipase A 2 from Trimeresurus flavoviridis venom

Toxicon ◽  
2001 ◽  
Vol 39 (7) ◽  
pp. 1069-1076 ◽  
Author(s):  
Yoko Yamaguchi ◽  
Yasuyuki Shimohigashi ◽  
Takahito Chijiwa ◽  
Makoto Nakai ◽  
Tomohisa Ogawa ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Phospholipase A ◽  
Trimeresurus Flavoviridis ◽  
Phospholipase A 2

Partial amino acid sequence of the basic crotalus phospholipase A

Toxicon ◽  
1975 ◽  
Vol 13 (1) ◽  
pp. 69-71 ◽  
Author(s):  
Tamotsu Omori-Satoh ◽  
J. Lang ◽  
H. Breithaupt ◽  
E. Habermann
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Phospholipase A ◽  
Partial Amino Acid Sequence

Partial amino acid sequence of snake venom phospholipase A

1970 ◽  
Vol 221 (2) ◽  
pp. 417-420 ◽  
Author(s):  
Yuji Samejima ◽  
Sadaaki Iwanaga ◽  
Tomoji Suzuki ◽  
Saju Kawauchi
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Snake Venom ◽  
Phospholipase A ◽  
Partial Amino Acid Sequence ◽  
Snake Venom Phospholipase

The staining pattern of the tropomyosin sequence is displayed in a new paracrystal

1986 ◽  
Vol 44 ◽  
pp. 150-151
Author(s):  
M.K. Lamvik ◽  
L.L. Klatt
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Staining Pattern ◽  
Banding Patterns ◽  
Mass Thickness ◽  
New Form

Tropomyosin paracrystals have been used extensively as test specimens and magnification standards due to their clear periodic banding patterns. The paracrystal type discovered by Ohtsuki1 has been of particular interest as a test of unstained specimens because of alternating bands that differ by 50% in mass thickness. While producing specimens of this type, we came across a new paracrystal form. Since this new form displays aligned tropomyosin molecules without the overlaps that are characteristic of the Ohtsuki-type paracrystal, it presents a staining pattern that corresponds to the amino acid sequence of the molecule.

Isolation and Structural Charaderization of a Potent Inhibitor of Coagulation Factor Xa from the Leech Haementeria ghilianii

1989 ◽  
Vol 61 (03) ◽  
pp. 437-441 ◽  
Author(s):  
Cindra Condra ◽  
Elka Nutt ◽  
Christopher J Petroski ◽  
Ellen Simpson ◽  
P A Friedman ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Salivary Gland ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Western Blot ◽  
Potent Inhibitor ◽  
Factor Xa ◽  
Coagulation Factor ◽  
Sds Page ◽  
Bovine Factor

SummaryThe present work reports the discovery and charactenzation of an anticoagulant protein in the salivary gland of the giant bloodsucking leech, H. ghilianii, which is a specific and potent inhibitor of coagulation factor Xa. The inhibitor, purified to homogeneity, displayed subnanomolar inhibition of bovine factor Xa and had a molecular weight of approximately 15,000 as deduced by denaturing SDS-PAGE. The amino acid sequence of the first 43 residues of the H. ghilianii derived inhibitor displayed a striking homology to antistasin, the recently described subnanomolar inhibitor of factor Xa isolated from the Mexican leech, H. officinalis. Antisera prepared to antistasin cross-reacted with the H. ghilianii protein in Western Blot analysis. These data indicate that the giant Amazonian leech, H. ghilianii, and the smaller Mexican leech, H. officinalrs, have similar proteins which disrupt the normal hemostatic clotting mechanisms in their mammalian host’s blood.

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