Sequence of the first 234 amino acids of porcine pancreatic lipase
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چکیده
منابع مشابه
The amino-terminal sequence of porcine pepsinogen.
Amino acid sequence studies were performed on (a) peptides obtained from tryptic hydrolysates of succinyl pepsinogen and (b) those isolated from a peptide mixture formed when pepsinogen is activated to pepsin. These peptides taken together with tryptic peptides obtained from reduced carboxymethylated pepsinogen establish the complete sequence of 41 residues at the NH&erminal end of the single p...
متن کاملconjugated linoleic acids, amino acid profile and other characteristics of meat produced under identical condition from two iranian fat tailed breeds of lamb
گوشت قرمز یکی از مهم ترین فرآورده های دامی در تأمین پروتئین و انرژی می باشد که در حمل ویتامین های محلول در چربی نیز حائز اهمیت می باشد. انسان مانند سایر مهره داران اسید های چرب ضروری (لینولئیک و آلفا لینولنیک) مورد نیاز خود از طریق غذا تأمین می نماید. اسید های چرب ضروی پیش ساز اسید های چرب غیر اشباع با چند پیوند دوگانه هستند. اسید لینولنیک پیش ساز اسیدهای چرب امگا 3 و اسید لینولئیک نیز پیش ساز ...
Effective Biodegradation of Mycotoxin Patulin by Porcine Pancreatic Lipase
Patulin is a common contaminant in fruits and vegetables, which is difficult to remove. In this study, the biodegradation of patulin using porcine pancreatic lipase (PPL) was investigated. The method of HPLC was used to analyze the concentration of patulin. Batch degradation experiments were performed to illustrate the effect of PPL amount, pH, temperature, contact time, and initial concentrati...
متن کاملAmino acid sequence of porcine neurophysin-I.
Tryptic and chymotryptic peptide fragments obtained from performic acid-oxidized porcine neurophysin-I were isolated and purified by gel filtration, ion exchange chromatography, paper electrophoresis, and paper chromatography. The larger tryptic peptides were further hydrolyzed by papain, chymotrypsin, pepsin, or HCl to yield shorter fragments amenable to Edman degradation. The sum of the compo...
متن کاملAmino-acid sequence of porcine pepsin.
As the culmination of several years of experiments, we propose a complete amino-acid sequence for porcine pepsin, an enzyme containing 327 amino-acid residues in a single polypeptide chain. In the sequence determination, the enzyme was treated with cyanogen bromide. Five resulting fragments were purified. The amino-acid sequence of four of the fragments accounted for 290 residues. Because the s...
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ژورنال
عنوان ژورنال: European Journal of Biochemistry
سال: 1979
ISSN: 0014-2956,1432-1033
DOI: 10.1111/j.1432-1033.1979.tb13127.x