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Trypsinogen-2 and trypsinogen activation peptide (TAP) in urine of patients with acute pancreatitis

Journal of Surgical Research, 2003
There is an obvious clinical need for a simple test that can identify patients at risk of developing severe acute pancreatitis. In this work we compared urinary trypsinogen-2 with urinary trypsinogen activation peptide (TAP) and serum C-reactive protein (CRP) for early differentiation between mild and severe acute pancreatitis.The study population ...
Ulf-Håkan Stenman   +2 more
exaly   +3 more sources

SYMMETRY PATTERNS IN TRYPSINOGEN

International Journal of Peptide and Protein Research, 1977
When the primary structure of bovine trypsinogen is searched for the existence of regularities, according to Greller & Erhan (1974), one finds eight pairs of peptides, arranged in a symmetrical pattern along the molecule. These peptides cover 49% of the length of the molecule–112 of the 227 amino acids – and each pair folds in a similar way.
S, Erhan, L D, Greller, B, Rasco
openaire   +2 more sources

Trypsinogen Deficiency Disease

Archives of Pediatrics & Adolescent Medicine, 1967
TOWNES,1in 1965, reported a 6-week-old white male infant with chronic diarrhea, failure to gain weight, hypoproteinemia, and edema. The infant was unable to hydrolyze dietary protein due to a singular deficiency of pancreatic trypsinogen. The present report describes a second instance of this interesting defect.
M D, Morris, D A, Fisher
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Comparison of the Partial Amino-acid Sequence of Dogfish Trypsinogen with Bovine Trypsinogen

Nature, 1970
Trypsinogen molecules from two species of different evolutionary periods are compared. Homology has been established by the sequencing of over half the amino-acids of the dogfish enzyme.
R A, Bradshaw   +4 more
openaire   +2 more sources

Cationic Trypsinogen Mutations and Pancreatitis

Clinics in Laboratory Medicine, 2004
The discovery of PRSS 1 mutations in hereditary pancreatitis and analysis of how the genotype affects the presentation and progression of hereditary pancreatitis has led to a better understanding of the pathophysiology of the disease. Patients with hereditary pancreatitis present with symptoms at an early age and have a significant lifetime risk for ...
Howes N   +3 more
openaire   +5 more sources

The Molecular Evolution of the Vertebrate Trypsinogens

Journal of Molecular Evolution, 1997
We expand the already large number of known trypsinogen nucleotide and amino acid sequences by presenting additional trypsinogen sequences from the tunicate (Boltenia villosa), the lamprey (Petromyzon marinus), the pufferfish (Fugu rubripes), and the frog (Xenopus laevis). The current array of known trypsinogen sequences now spans the entire vertebrate
J C, Roach, K, Wang, L, Gan, L, Hood
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Trypsinogen Mutations in Pancreatic Disorders

Endocrinology and Metabolism Clinics of North America, 2006
There are multiple PRSS1 mutations described in hereditary pancreatitis but only a minority of these are clinically relevant. The two most frequent point mutations are in exon 2 (N29I) and exon3 (R122H), found in diverse racial populations. Both mutations result in early onset pancreatitis but the mechanism underlying this phenotype is unclear.
Louis J, Vitone   +4 more
openaire   +2 more sources

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