PURIFICATION AND PHYSICAL PROPERTIES OF GROUP C STREPTOCOCCAL PHAGE-ASSOCIATED LYSIN

Fischetti , Vincent A.; Gotschlich , Emil C.; Bernheimer , Alan W.

doi:10.1084/jem.133.5.1105

Article navigation

Article| May 01 1971

PURIFICATION AND PHYSICAL PROPERTIES OF GROUP C STREPTOCOCCAL PHAGE-ASSOCIATED LYSIN

Vincent A. Fischetti,

Vincent A. Fischetti

From the Department of Microbiology, New York University School of Medicine, New York 10016, and The Rockefeller University, New York 10021

Search for other works by this author on:

This Site

PubMed

Google Scholar

Emil C. Gotschlich,

Emil C. Gotschlich

From the Department of Microbiology, New York University School of Medicine, New York 10016, and The Rockefeller University, New York 10021

Search for other works by this author on:

This Site

PubMed

Google Scholar

Alan W. Bernheimer

From the Department of Microbiology, New York University School of Medicine, New York 10016, and The Rockefeller University, New York 10021

Search for other works by this author on:

This Site

PubMed

Google Scholar

Author and Article Information

Vincent A. Fischetti

From the Department of Microbiology, New York University School of Medicine, New York 10016, and The Rockefeller University, New York 10021

Emil C. Gotschlich

From the Department of Microbiology, New York University School of Medicine, New York 10016, and The Rockefeller University, New York 10021

Alan W. Bernheimer

From the Department of Microbiology, New York University School of Medicine, New York 10016, and The Rockefeller University, New York 10021

Received: January 14 1971

Online ISSN: 1540-9538

Print ISSN: 0022-1007

1971

J Exp Med (1971) 133 (5): 1105–1117.

https://doi.org/10.1084/jem.133.5.1105

A purification procedure for the Group C phage-associated lysin is described utilizing tetrathionate to protect the enzyme's -SH group(s) from thiol-inactivating agents. A 652-fold purification has been accomplished yielding a solution in which the enzyme activity corresponds to essentially a single band on polyacrylamide gel which accounts for 70% of the total protein in the preparation. A molecular weight of 101,000 and frictional ratio of 1.526 was determined for the lysin utilizing experimentally determined values for its Stokes radius and sedimentation coefficient.

This content is only available as a PDF.

1971

You do not currently have access to this content.

Don't already have an account? Register

You could not be signed in. Please check your email address / username and password and try again.

PURIFICATION AND PHYSICAL PROPERTIES OF GROUP C STREPTOCOCCAL PHAGE-ASSOCIATED LYSIN

Sign in

Client Account

Sign in via your Institution

Suggested Content

Email alerts

This Feature Is Available To Subscribers Only