Expression, Purification, and Characterization of the Recombinant Pepsin Inhibitor from Ascaris suum

1998 ◽  
pp. 387-389 ◽  
Author(s):  
Jeffrey Zalatoris ◽  
Chetana Rao-Naik ◽  
Gregory Fecho ◽  
Karen Girdwood ◽  
John Kay ◽  
...  
Keyword(s):  
Ascaris Suum ◽  
Purification And Characterization ◽  
Pepsin Inhibitor

Expression, purification and characterization of refolded rBm-33 (pepsin inhibitor homolog) from Brugia malayi: A human Lymphatic Filarial parasite

2011 ◽  
Vol 79 (2) ◽  
pp. 245-250 ◽  
Author(s):  
Nagampalli Raghavendra Sashi Krishna ◽  
N.S.A. Krushna ◽  
R.B. Narayanan ◽  
S.S. Rajan ◽  
K. Gunasekaran
Keyword(s):  
Brugia Malayi ◽  
Filarial Parasite ◽  
Purification And Characterization ◽  
Pepsin Inhibitor

scholarly journals Purification and characterization of alpha-amylases from the intestine and muscle of ascaris suum (Nematoda).

2001 ◽  
Vol 48 (3) ◽  
pp. 763-774 ◽  
Author(s):  
K Zółtowska
Keyword(s):  
Molecular Mass ◽  
Isoelectric Focusing ◽  
Ascaris Suum ◽  
Iodoacetic Acid ◽  
Maximum Activity ◽  
Alpha Amylase ◽  
Purification And Characterization ◽  
Muscle Enzyme ◽  
Sds Page

Alpha-Amylase (EC 3.2.1.1) was purified from the muscle and intestine of the parasitic helminth of pigs Ascaris suum. The enzymes from the two sources differed in their properties. Isoelectric focusing revealed one form of a-amylase from muscles with pl of 5.0, and two forms of amylase from intestine with pI of 4.7 and 4.5. SDS/PAGE suggested a molecular mass of 83 kDa and 73 kDa for isoenzymes of a-amylases from intestine and 59 kDa for the muscle enzyme. Alpha-Amylase from intestine showed maximum activity at pH 7.4, and the enzyme from muscle at pH 8.2. The muscle enzyme was more thermostabile than the intestinal alpha-amylase. Both the muscle and intestine amylase lost half of its activity after 15 min at 70 degrees C and 50 degrees C, respectively. The Km values were: for muscle amylase 0.22 microg/ml glycogen and 3.33 microg/ml starch, and for intestine amylase 1.77 microg/ml glycogen and 0.48 microg/ml starch. Both amylases were activated by Ca2+ and inhibited by EDTA, iodoacetic acid, p-chloromercuribenzoate and the inhibitor of a-amylase from wheat. No significant differences were found between the properties of a-amylases from parasites and from their hosts.

Purification and characterization of phosphorylase B from Ascaris suum

1983 ◽  
Vol 9 (4) ◽  
pp. 297-307 ◽  
Author(s):  
Nuha J. Yacoub ◽  
Benja L. Allen ◽  
D.Michael Payne ◽  
Ruthann A. Masaracchia ◽  
Ben G. Harris
Keyword(s):  
Ascaris Suum ◽  
Purification And Characterization
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