Abstract
1. 1. Silky and lemon shark muscle glycogen phosphorylases b and a were purified and crystallized under similar conditions. In contrast to other phosphorylases, both enzymes crystallize from ammonium sulphate or buffer. The doubling in molecular weight observed upon phosphorylation to the a form is similar to that of homoiothenns but different from that of other poikilotherms (frog and lobster). 2. 2. The enzymes from these a shark species are more stable than those from muscle of homoiotherms and, like lobster phosphorylase, they require no sulphydryl compounds for maintaining their activity. 3. 3. Lemon and silky shark phosphorylases appear to be immunologically identical and distinct from the phosphorylases of rabbit or human muscle. 4. 4. The fact that phosphorylase from lemon or silky shark can be prepared in homogenous form, crystallized, and stabilized in dilute buffer without need for the activator 5/-AMP, sulphydryl compounds, or a high concentration of salts, makes it unique among the glycogen phosphorylases and particularly useful for research purposes.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 604-608 |
| Number of pages | 5 |
| Journal | International Journal of Biochemistry |
| Volume | 2 |
| Issue number | 11 |
| DOIs | |
| State | Published - 1971 |
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Keywords
- Carcharhinus faiciformis
- comparative studies on glycogen phosphorylase of poikilotherms and homoiotherms
- crystallization
- immunological behaviour
- JVegaprion brevirostris
- lemon shark
- molecular weight
- Silky shark
- solubility
- stability
- sulphydryl groups
ASJC Scopus subject areas
- Biochemistry
Cite this
A comparative study of crystallized silky and lemon shark muscle glycogen phosphorylases. / Assaf, Sáid A.; Yunis, Adel A.
In: International Journal of Biochemistry, Vol. 2, No. 11, 1971, p. 604-608.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - A comparative study of crystallized silky and lemon shark muscle glycogen phosphorylases
AU - Assaf, Sáid A.
AU - Yunis, Adel A
PY - 1971
Y1 - 1971
N2 - 1. 1. Silky and lemon shark muscle glycogen phosphorylases b and a were purified and crystallized under similar conditions. In contrast to other phosphorylases, both enzymes crystallize from ammonium sulphate or buffer. The doubling in molecular weight observed upon phosphorylation to the a form is similar to that of homoiothenns but different from that of other poikilotherms (frog and lobster). 2. 2. The enzymes from these a shark species are more stable than those from muscle of homoiotherms and, like lobster phosphorylase, they require no sulphydryl compounds for maintaining their activity. 3. 3. Lemon and silky shark phosphorylases appear to be immunologically identical and distinct from the phosphorylases of rabbit or human muscle. 4. 4. The fact that phosphorylase from lemon or silky shark can be prepared in homogenous form, crystallized, and stabilized in dilute buffer without need for the activator 5/-AMP, sulphydryl compounds, or a high concentration of salts, makes it unique among the glycogen phosphorylases and particularly useful for research purposes.
AB - 1. 1. Silky and lemon shark muscle glycogen phosphorylases b and a were purified and crystallized under similar conditions. In contrast to other phosphorylases, both enzymes crystallize from ammonium sulphate or buffer. The doubling in molecular weight observed upon phosphorylation to the a form is similar to that of homoiothenns but different from that of other poikilotherms (frog and lobster). 2. 2. The enzymes from these a shark species are more stable than those from muscle of homoiotherms and, like lobster phosphorylase, they require no sulphydryl compounds for maintaining their activity. 3. 3. Lemon and silky shark phosphorylases appear to be immunologically identical and distinct from the phosphorylases of rabbit or human muscle. 4. 4. The fact that phosphorylase from lemon or silky shark can be prepared in homogenous form, crystallized, and stabilized in dilute buffer without need for the activator 5/-AMP, sulphydryl compounds, or a high concentration of salts, makes it unique among the glycogen phosphorylases and particularly useful for research purposes.
KW - Carcharhinus faiciformis
KW - comparative studies on glycogen phosphorylase of poikilotherms and homoiotherms
KW - crystallization
KW - immunological behaviour
KW - JVegaprion brevirostris
KW - lemon shark
KW - molecular weight
KW - Silky shark
KW - solubility
KW - stability
KW - sulphydryl groups
UR - http://www.scopus.com/inward/record.url?scp=49649152469&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=49649152469&partnerID=8YFLogxK
U2 - 10.1016/0020-711X(71)90032-2
DO - 10.1016/0020-711X(71)90032-2
M3 - Article
VL - 2
SP - 604
EP - 608
JO - International Journal of Biochemistry and Cell Biology
JF - International Journal of Biochemistry and Cell Biology
SN - 1357-2725
IS - 11
ER -