Preparation and Properties of Crystalline Salmon Pepsin*
نویسنده
چکیده
The techniques of crystallization, developed in recent years, have permitted enzyme studies that are far more exact than were possible with the more crude preparations. Among the crystalline enzymes, Northrop’s pepsin has been the object of widespread and intensive research (1) which has contributed to the knowledge of enzyme action and mode of operation. In order to further the understanding of pepsin, it seemed worth while to begin comparative studies on pepsins from sources other than beef and swine. In the work to be described the pepsin of the Pacific Coast king salmon (Oncorhynchus tschawytscha) was crystallized, and comparative studies have been begun. Methods for crystallizing swine pepsin have been described by Northrop (2) and Philpot (3). Fortunately, the techniques for handling mammalian pepsin and pepsinogen (4) have been found applicable, with some modification, to fish pepsin. g!Most of th e s used as sources of material were caught in fi h traps at La Conner, Washington, and brought under ice to Seattle, where they were dressed, after having been about 18 hours out of water. The stomachs were removed, cleaned, and stored frozen; about 100 were required for each kilo of mucosa. The stomachs from actively feeding fish, caught at sea, were larger and contained more pepsin, but were difficult to ship successfully to Seattle.
منابع مشابه
Inactivation of Pepsin by Iodine
1. Pepsin solutions were iodinated at pH 5.0-6.0 until 10-20 per cent of the activity was lost and 1/20 (0.7 per cent) of the saturating amount of iodine had been introduced into the protein molecule. After alkaline hydrolysis 65 per cent of the original iodine was accounted for as mono-iodotyrosine although only 42 per cent was isolated as a crystalline product. No evidence was obtained to sup...
متن کاملIsolation, Crystallization, and Properties of Swine Pepsinogen
1. A method is described for the preparation of pepsinogen from swine gastric mucosae which consists of extraction and fractional precipitation with ammonium sulfate solutions followed by two precipitations with a copper hydroxide reagent under particular conditions. Crystallization as very thin needles takes place at 10 degrees C., pH 5.0 and from 0.4 saturated ammonium sulfate solution contai...
متن کاملThe heat-inactivation of crystalline pepsin; the critical increment of the process.
IN a recent series of publications Northrop [1930, 1, 2; 1931] has advanced very strong evidence that pepsin is a protein. Starting from commercial pepsin, by suitably regulating the pH and precipitating with the aid of magnesium or ammonium sulphate a crystalline product was obtained which had the general properties of a protein. In particular, solutions of this crystalline pepsin were coagula...
متن کاملPreparation and Characterization of Pullulan-Soy Protein Concentrate Biocomposite Film
The non-biodegradable nature of plastic packaging has brought about an attention in bio-basedpackaging materials. Edible composite films were prepared using soy protein concentrate (SPC) and pullulan(PUL) biopolymer at five different ratio (100:0; 70:30; 50:50; 30:70 and 0:100) with glycerol as plasticizer bycasting-evaporation method. The thickness, mechanical properties, water vapor permeabil...
متن کاملCrystalline Acetyl Derivatives of Pepsin
Crystalline pepsin has been acetylated by the action of ketene in aqueous solution at pH 4.07-5.5. As acetylation proceeds the activity decreases, the decrease being more rapid at pH 5.0-5.5 than at 4.0-4.5. Three acetyl derivatives have been isolated from the reaction mixture and obtained in crystalline form. The crystal form of these derivatives is similar to that of pepsin. Fractionation and...
متن کامل