Literature DB >> 19873264

INACTIVATION OF PEPSIN BY IODINE : II. ISOLATION OF CRYSTALLINEl-MONO-IODOTYROSINE FROM PARTIALLY IODINATED PEPSIN.

R M Herriott1.   

Abstract

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 support the possibility that any group other than tyrosine in pepsin was iodinated. 2. Some of the properties of the crystalline l-mono-iodotyrosine were determined and compared to those of di-iodotyrosine. 3. One iodinated pepsin preparation was crystallized. The crystal form was the same as that of the original pepsin. A solubility curve of the crystals demonstrated that it was very different from pepsin and had nearly constant solubility.

Entities:  

Year:  1941        PMID: 19873264      PMCID: PMC2142046          DOI: 10.1085/jgp.25.2.185

Source DB:  PubMed          Journal:  J Gen Physiol        ISSN: 0022-1295            Impact factor:   4.086


  1 in total

1.  The actions of iodine and hypoiodous acid on pepsin.

Authors:  J S Philpot; P A Small
Journal:  Biochem J       Date:  1939-10       Impact factor: 3.857

  1 in total
  1 in total

1.  [Inactivation of the thyroid-stimulating and exophthalmogenic effect of TSH, LATS, EPF, thyroid antibodies and serum protein fractions by iodine].

Authors:  K Schemmel; D Streich; G Kreysing; K Leybold; L Weisbecker
Journal:  Klin Wochenschr       Date:  1969-08-15
  1 in total

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