INT63499

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Context Info
Confidence 0.88
First Reported 1996
Last Reported 2007
Negated 3
Speculated 0
Reported most in Abstract
Documents 3
Total Number 4
Disease Relevance 0.47
Pain Relevance 0

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extracellular space (AMY2A) small molecule metabolic process (AMY2A) hydrolase activity, acting on glycosyl bonds (AMY2A)
extracellular region (AMY2A) carbohydrate metabolic process (AMY2A)
AMY2A (Homo sapiens)
Pain Link Frequency Relevance Heat
Paracetamol 2 44.96 Quite Low
Chronic pancreatitis 2 25.00 Low Low
Disease Link Frequency Relevance Heat
Calcification 2 81.12 Quite High
Pancreatitis 10 80.40 Quite High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
By further incubation for 24 h, glycoprotein-1, procarboxypeptidase A-1 and lipase were nearly completely degraded, while alpha-amylase and procarboxypeptidase B-1 were not degraded under these conditions; alpha-amylase became labile in the presence of 1 mM ethylene diaminetetraacetic acid (EDTA) or 10 mM phenyl methyl sulfonyl fluoride (PMSF).
Neg (not) Protein_catabolism (degraded) of alpha-amylase
1) Confidence 0.88 Published 1996 Journal Electrophoresis Section Abstract Doc Link 8738347 Disease Relevance 0.23 Pain Relevance 0
Amylose-based polymers are normally subject to biodegradation by alpha-amylase enzymes present in the gastrointestinal tract, but matrix systems show no significant degradation of tablets by alpha-amylase in vitro.
Protein_catabolism (biodegradation) of alpha-amylase
2) Confidence 0.86 Published 2007 Journal Eur J Pharm Biopharm Section Abstract Doc Link 17275270 Disease Relevance 0 Pain Relevance 0
Amylose-based polymers are normally subject to biodegradation by alpha-amylase enzymes present in the gastrointestinal tract, but matrix systems show no significant degradation of tablets by alpha-amylase in vitro.
Neg (no) Protein_catabolism (degradation) of alpha-amylase
3) Confidence 0.86 Published 2007 Journal Eur J Pharm Biopharm Section Abstract Doc Link 17275270 Disease Relevance 0 Pain Relevance 0
By further incubation for 24 h, glycoprotein-1, procarboxypeptidase A-1 and lipase were nearly completely degraded, while alpha-amylase and procarboxypeptidase B-1 were not degraded under these conditions; alpha-amylase became labile in the presence of 1 mM ethylene diaminetetraacetic acid (EDTA) or 10 mM phenyl methyl sulfonyl fluoride (PMSF).
Neg (not) Protein_catabolism (degraded) of alpha-amylase
4) Confidence 0.58 Published 1996 Journal Electrophoresis Section Abstract Doc Link 8738347 Disease Relevance 0.24 Pain Relevance 0

General Comments

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