1962
DOI: 10.1007/bf00682376
|View full text |Cite
|
Sign up to set email alerts
|

Strukturchemische Untersuchungen �ber den Aufbau des wasserunl�slichen Eiwei�es klarer Rinderlinsen

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...

Citation Types

0
1
0

Year Published

1965
1965
1976
1976

Publication Types

Select...
3
3

Relationship

0
6

Authors

Journals

citations
Cited by 15 publications
(1 citation statement)
references
References 13 publications
0
1
0
Order By: Relevance
“…Structural methods are useful in the characterization of proteins lacking a characteristic biological property, and have the advantage that alterations during isolation are more likely to affect the conformation than the primary structure. a-Crystallin, which comprises about a third of the soluble lens proteins and is closely related to the insoluble protein albuminoid (Woods & Burky, 1927;Thomann, 1962;Ruttenberg, 1965;Waley, 1965b), contains 1 thiol group/sub-unit (Waley, 1965a). This feature has now been utilized in comparisons of a-crystallin with other lens proteins, and forms the basis for a chemical method of recognizing oc-crystallin.…”
mentioning
confidence: 99%
“…Structural methods are useful in the characterization of proteins lacking a characteristic biological property, and have the advantage that alterations during isolation are more likely to affect the conformation than the primary structure. a-Crystallin, which comprises about a third of the soluble lens proteins and is closely related to the insoluble protein albuminoid (Woods & Burky, 1927;Thomann, 1962;Ruttenberg, 1965;Waley, 1965b), contains 1 thiol group/sub-unit (Waley, 1965a). This feature has now been utilized in comparisons of a-crystallin with other lens proteins, and forms the basis for a chemical method of recognizing oc-crystallin.…”
mentioning
confidence: 99%