Proteolysis of tropoelastin.

R. Mecham; J. A. Foster; C. Franzblau

doi:10.1007/978-1-4684-9093-0_18

Proteolysis of tropoelastin.

R. Mecham
, J. A. Foster
, C. Franzblau

Research output: Contribution to journal › Article › peer-review

3 Scopus citations

Abstract

The presence of an enzyme associated with tropoelastin is described. The enzyme has a pH optimum between 7 and 9 and trypsin-like specificity. Upon incubation, tropoelastin (72,000 molecular weight) is cleaved into relatively high molecular weight fragments. In addition to the parent molecule, five discrete polypeptide bands are usually observed on SDS gels with molecular weights of approximately 57,000, 45,000, 36,000, 25,000 and 13-14,000.

Original language	English
Pages (from-to)	209-220
Number of pages	12
Journal	Advances in Experimental Medicine and Biology
Volume	79
DOIs	https://doi.org/10.1007/978-1-4684-9093-0_18
State	Published - 1977

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@article{005e5bd339b0480a966721c368891887,

title = "Proteolysis of tropoelastin.",

abstract = "The presence of an enzyme associated with tropoelastin is described. The enzyme has a pH optimum between 7 and 9 and trypsin-like specificity. Upon incubation, tropoelastin (72,000 molecular weight) is cleaved into relatively high molecular weight fragments. In addition to the parent molecule, five discrete polypeptide bands are usually observed on SDS gels with molecular weights of approximately 57,000, 45,000, 36,000, 25,000 and 13-14,000.",

author = "R. Mecham and Foster, \{J. A.\} and C. Franzblau",

year = "1977",

doi = "10.1007/978-1-4684-9093-0\_18",

language = "English",

volume = "79",

pages = "209--220",

journal = "Advances in Experimental Medicine and Biology",

issn = "0065-2598",

}

TY - JOUR

T1 - Proteolysis of tropoelastin.

AU - Mecham, R.

AU - Foster, J. A.

AU - Franzblau, C.

PY - 1977

Y1 - 1977

N2 - The presence of an enzyme associated with tropoelastin is described. The enzyme has a pH optimum between 7 and 9 and trypsin-like specificity. Upon incubation, tropoelastin (72,000 molecular weight) is cleaved into relatively high molecular weight fragments. In addition to the parent molecule, five discrete polypeptide bands are usually observed on SDS gels with molecular weights of approximately 57,000, 45,000, 36,000, 25,000 and 13-14,000.

AB - The presence of an enzyme associated with tropoelastin is described. The enzyme has a pH optimum between 7 and 9 and trypsin-like specificity. Upon incubation, tropoelastin (72,000 molecular weight) is cleaved into relatively high molecular weight fragments. In addition to the parent molecule, five discrete polypeptide bands are usually observed on SDS gels with molecular weights of approximately 57,000, 45,000, 36,000, 25,000 and 13-14,000.

UR - https://www.scopus.com/pages/publications/0017443401

U2 - 10.1007/978-1-4684-9093-0_18

DO - 10.1007/978-1-4684-9093-0_18

M3 - Article

C2 - 868636

AN - SCOPUS:0017443401

SN - 0065-2598

VL - 79

SP - 209

EP - 220

JO - Advances in Experimental Medicine and Biology

JF - Advances in Experimental Medicine and Biology

ER -

Proteolysis of tropoelastin.

Abstract

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