A Thiol Dependent Acid Protease View Full Text


Ontology type: schema:Chapter     


Chapter Info

DATE

1977

AUTHORS

T. Turnšek , I. Kregar , D. Lebez , V. Turk

ABSTRACT

It is a well known fact that lysosornes have an adequate complement of proteolytic enzymes for intracellular protein degradation. However, little is known about the steps that occur during such proteolysis, the total number and nature of the enzymes involved or their possible concerted action. A pathway of protein hydrolysis by lysosomal enzymes was proposed (1,2) in which acid proteases attack proteins to produce oligopeptides that are then digested to completion by exopeptidases and dipeptidases. Our experiments were aimed to investigate the number and nature of acid endopeptidases present in calf lymph nodes. This tissue was used as a source of the cathepsins, because it has been suggested that, along with cathepsins B and C, at least two different acid proteases could be responsible for the hydrolysis of hemoglobin and albumin as reported by Stein and Fruton (3). Fräkki et. al. (4) measuring the digestion of endogenous tissue proteins, hemoglobin and casein by crude rat thymus and lymph nodes’ extracts, proposed that the whole proteolytic activity consists of several separate enzymes with different pH optima. More... »

PAGES

290-298

Book

TITLE

Intracellular Protein Catabolism II

ISBN

978-1-4615-8815-3
978-1-4615-8813-9

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/978-1-4615-8813-9_37

DOI

http://dx.doi.org/10.1007/978-1-4615-8813-9_37

DIMENSIONS

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