Isozymes of α-amylase in the porcine pancreas: Population distribution

Strumeyer, David H.; Kao, Wei-Chun; Roberts, Terry; Forsyth-Davis, D.

doi:10.1016/0305-0491(88)90153-8

Cited by 4 publications

(3 citation statements)

References 23 publications

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“…In mammals, these genes code for salivary and pancreatic a-amylases (Robins & Samuelson, 1992). As a consequence of the gene size and multitude of alleles, polymorphism of a-amylases is observed even among individuals belonging to the same species (Nebinger, 1986;Strumeyer et al, 1988;McMahon et al, 1999;Terziè et al, 1999). From two to six isoenzymatic forms dif- The enzymes were preincubated in 1.0 ml of veronal/Na acetate buffer, pH 7.4 or 8.4 for 15 min at 37°C with each of the effectors before the addition of substrate.…”

Section: Discussionmentioning

confidence: 99%

“…fering more or less in their physical, chemical and immunological properties can be simultaneously present (Strumeyer et al, 1988;Anindyawati et al, 1998;Fereyroux et al, 1998;Ferrer et al, 1999;Matsuo et al, 1999). Similarly, in A. suum at least three a-amylases differing in their properties -pseudocoelomic ( enka & Prokopiè, 1984), muscle and intestinal -were found.…”

Section: Discussionmentioning

confidence: 99%

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

Zoltowska¹

2001

Acta Biochim Pol

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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.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

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

Zoltowska¹

2001

Acta Biochim Pol

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“…2A). Three bands are expected for porcine aamylase 2 (Strumeyer et al 1988). Cebidichthys violaceus (aamylase 2A pI 7.86), P. chirus (a-amylase 2 pI 7.59), X. mucosus (a-amylase 2 pI 7.73), and X. atropurpureus (a-amylase 2 pI 7.32) were run under common conditions, with a single band visible for each of them ( fig.…”

Section: Polyacrylamide Gel Electrophoresismentioning

confidence: 99%

Elevated Gene Copy Number Does Not Always Explain Elevated Amylase Activities in Fishes

German

Foti

Heras

et al. 2016

Physiological and Biochemical Zoology

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Amylase activity variation in the guts of several model organisms appears to be explained by amylase gene copy number variation. We tested the hypothesis that amylase gene copy number is always elevated in animals with high amylolytic activity. We therefore sequenced the amylase genes and examined amylase gene copy number in prickleback fishes (family Stichaeidae) with different diets including two species of convergently evolved herbivores with the elevated amylase activity phenotype. We found elevated amylase gene copy number (six haploid copies) with sequence variation among copies in one herbivore (Cebidichthys violaceus) and modest gene copy number (two to three haploid copies) with little sequence variation in the remaining taxa, which included herbivores, omnivores, and a carnivore. Few functional differences in amylase biochemistry were observed, and previous investigations showed similar digestibility among the convergently evolved herbivores with differing amylase genetics. Hence, the phenotype of elevated amylase activity can be achieved by different mechanisms (i.e., elevated expression of fewer genes, increased gene copy number, or expression of more efficient amylase proteins) with similar results. Phylogenetic and comparative genomic analyses of available fish amylase genes show mostly lineage-specific duplication events leading to gene copy number variation, although a whole-genome duplication event or chromosomal translocation may have produced multiple amylase copies in the Ostariophysi, again showing multiple routes to the same result.

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The Structure and Metabolism of Carbohydrates

Urich

1994

Comparative Animal Biochemistry

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Isozymes of α-amylase in the porcine pancreas: Population distribution

Cited by 4 publications

References 23 publications

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

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

Elevated Gene Copy Number Does Not Always Explain Elevated Amylase Activities in Fishes

The Structure and Metabolism of Carbohydrates

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