First published online November 28, 2008
Journal of Experimental Biology 211, 3767-3774 (2008)
Published by The Company of Biologists 2008
doi: 10.1242/jeb.023754
Digestive physiology of the Burmese python: broad regulation of integrated performance
Stephen M. Secor
Department of Biological Sciences, The University of Alabama, Tuscaloosa,
AL 35405, USA

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Fig. 1. (A) A Burmese python swallowing a laboratory rat which it had killed by
constriction. (B) A Burmese python 24 h after consuming a rat meal greater
than 50% of the snake's body mass. This snake had experienced further
distension of its body after feeding due to the build up of gases within the
ingested dead rat.
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Fig. 2. (A) Daily X-ray images of a python digesting a rat that was equal to 25% of
the snake's body mass. At 1 day postfeeding (DPF), the rat's skeleton is
completely intact within the python's stomach, whereas by day 6 the rat's
skeleton has been completely broken down and passed into the small intestine.
(B) The postprandial profile of gastric pH for Burmese pythons demonstrating
the rapid drop in pH after feeding, the steady maintenance of a very acidic pH
during digestion, and the rise in pH upon the completion of gastric digestion
when acid production ceases. Error bars in B and subsequent figures represent
±1 s.e.m. Gastric pH profile redrawn from data presented in Secor
(Secor, 2003 ).
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Fig. 3. Transmission electron micrographs illustrating the rapid postprandial
lengthening of the python's intestinal microvilli, reaching a peak in length
at 3 days postfeeding. After digestion is complete (after day 6), the
microvilli shorten in length. Bar in images represent 1 µm.
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Fig. 4. Activities of the brushborder enzymes aminopeptidase-N (APN) and maltase,
and uptake rates of the amino acid L-proline and the sugar
D-glucose as a function of time postfeeding for the proximal region
of the Burmese python's small intestine. For both proteins and simple sugars,
pythons experience matched regulation of intestinal digestion and absorption.
Enzyme activity profiles taken from Cox and Secor
(Cox and Secor, 2008 ).
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Fig. 5. Images of the small intestine of similar-sized Burmese pythons fasted and
at 2 and 10 days postfeeding (DPF). By 2 DPF, the intestine has increased in
diameter due primarily to hypertrophy of the epithelial cells; a response that
has reversed by 10 DPF.
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Fig. 6. Plasma concentrations of cholecystokinin (CCK), glucose-dependent
insulinotropic peptide (GIP), glucagon and insulin as a function of time
postfeeding for the Burmese python. The dramatic postprandial release into
circulation of these regulatory peptides may serve to signal the upregulation
of tissue structure and function. Profiles of CCK, GIP and glucagon redrawn
from data presented in Secor et al. (Secor
et al., 2001 ).
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Fig. 7. Hypothetical model of the cellular mechanisms involved in the postprandial
lengthening of the python's intestinal microvilli and subsequent shortening of
the microvilli once digestion is complete. In this scenario, structural
proteins and vesicles of membrane sequestered within the cytoplasm during
fasting rapidly migrate to the apical membrane with feeding and are inserted
in place to further lengthen the existing microvilli. After digestion is
complete, the components of the microvilli are either released into the lumen
or return back to the cytosol for reuse.
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Fig. 9. Positron emission tomography (PET) images of a fasted and fed (1 day
postfeeding) Burmese python. Snakes were injected with
2-[18F]fluoro-2-deoxyglucose prior to scanning. Bright areas
signify regions experiencing high rates of glucose metabolism. The difference
between the two images is actually greater given that the intensity of the
fasted image had to be increased 1000-fold in order to view the entire
snake.
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Fig. 10. Wet mass of the heart, pancreas, liver and kidneys plotted against time
postfeeding for Burmese pythons fasted (0) and following the consumption of
rodent meals equal to 25% of the snake's body mass. Feeding generates
respective increases in wet mass of 40%, 94%, 106% and 72% for the heart,
pancreas, liver and kidneys.
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Fig. 11. Transmission electron micrograph of python intestinal epithelium embedded
with spherical particles composed of calcium and phosphate. It is hypothesized
that the source of the calcium and phosphate is the degraded skeleton of the
rodent meal (Lignot et al.,
2005 ). The bar in the image represents 1 µm.
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© The Company of Biologists Ltd 2008