Comparison of the nerve growth factor proteins from cobra venom (Naja naja) and mouse submaxillary gland

Alfred C. Server, Karl Herrup, Eric M. Shooter, Ruth A. Hogue-Angeletti, William A. Frazier, Ralph A. Bradshaw

Research output: Contribution to journalArticle

30 Citations (Scopus)

Abstract

The nerve growth factors (NGF's) isolated from cobra venom (Naja naja) and mouse submaxillary gland are closely related proteins. They are structurally similar in that about 60% of their amino acid residues are identical (Hogue-Angeletti, R. A., Frazier, W. A., Jacobs, J. W., Niall, H. D., and Bradshaw, R. A. (1976), Biochemistry, preceding paper in this issue). They are functionally similar in that they both elicit maximum neurite outgrowth from chick embryonic dorsal root ganglia at the same protein concentration. However, the extent of the response is not as great with Naja naja NGF. The cobra NGF has an affinity close to that of mouse NGF for a major proportion of the specific NGF receptors on cells from dissociated embryonic dorsal root ganglia. Despite these similarities there are differences which can be detected between the two proteins. High concentrations of Naja naja NGF will not displace approximately 20% of the binding of mouse NGF to specific NGF receptors. Moreover, Naja naja NGF shows limited cross-reactivity with antiserum to mouse NGF in a competition radioimmunoassay, consistent with the extent of its amino acid sequence homology with mouse NGF. Naja naja NGF does not interact with the α- and γ-subunits of 7S NGF to form a high molecular weight complex. In this behavior it resembles a modified form of mouse NGF which, like Naja naja NGF, lacks COOH-terminal arginine residues.

Original languageEnglish (US)
Pages (from-to)35-39
Number of pages5
JournalBiochemistry
Volume15
Issue number1
StatePublished - 1976
Externally publishedYes

Fingerprint

Cobra Venoms
Elapidae
Submandibular Gland
Nerve Growth Factors
Nerve Growth Factor
Proteins
Nerve Growth Factor Receptors
Spinal Ganglia
Amino Acids
Amino Acid Sequence Homology
Biochemistry
Radioimmunoassay
Arginine

ASJC Scopus subject areas

  • Biochemistry

Cite this

Server, A. C., Herrup, K., Shooter, E. M., Hogue-Angeletti, R. A., Frazier, W. A., & Bradshaw, R. A. (1976). Comparison of the nerve growth factor proteins from cobra venom (Naja naja) and mouse submaxillary gland. Biochemistry, 15(1), 35-39.

Comparison of the nerve growth factor proteins from cobra venom (Naja naja) and mouse submaxillary gland. / Server, Alfred C.; Herrup, Karl; Shooter, Eric M.; Hogue-Angeletti, Ruth A.; Frazier, William A.; Bradshaw, Ralph A.

In: Biochemistry, Vol. 15, No. 1, 1976, p. 35-39.

Research output: Contribution to journalArticle

Server, AC, Herrup, K, Shooter, EM, Hogue-Angeletti, RA, Frazier, WA & Bradshaw, RA 1976, 'Comparison of the nerve growth factor proteins from cobra venom (Naja naja) and mouse submaxillary gland', Biochemistry, vol. 15, no. 1, pp. 35-39.
Server AC, Herrup K, Shooter EM, Hogue-Angeletti RA, Frazier WA, Bradshaw RA. Comparison of the nerve growth factor proteins from cobra venom (Naja naja) and mouse submaxillary gland. Biochemistry. 1976;15(1):35-39.
Server, Alfred C. ; Herrup, Karl ; Shooter, Eric M. ; Hogue-Angeletti, Ruth A. ; Frazier, William A. ; Bradshaw, Ralph A. / Comparison of the nerve growth factor proteins from cobra venom (Naja naja) and mouse submaxillary gland. In: Biochemistry. 1976 ; Vol. 15, No. 1. pp. 35-39.
@article{9ffcd6b9ced547a89773fdcdf6215591,
title = "Comparison of the nerve growth factor proteins from cobra venom (Naja naja) and mouse submaxillary gland",
abstract = "The nerve growth factors (NGF's) isolated from cobra venom (Naja naja) and mouse submaxillary gland are closely related proteins. They are structurally similar in that about 60{\%} of their amino acid residues are identical (Hogue-Angeletti, R. A., Frazier, W. A., Jacobs, J. W., Niall, H. D., and Bradshaw, R. A. (1976), Biochemistry, preceding paper in this issue). They are functionally similar in that they both elicit maximum neurite outgrowth from chick embryonic dorsal root ganglia at the same protein concentration. However, the extent of the response is not as great with Naja naja NGF. The cobra NGF has an affinity close to that of mouse NGF for a major proportion of the specific NGF receptors on cells from dissociated embryonic dorsal root ganglia. Despite these similarities there are differences which can be detected between the two proteins. High concentrations of Naja naja NGF will not displace approximately 20{\%} of the binding of mouse NGF to specific NGF receptors. Moreover, Naja naja NGF shows limited cross-reactivity with antiserum to mouse NGF in a competition radioimmunoassay, consistent with the extent of its amino acid sequence homology with mouse NGF. Naja naja NGF does not interact with the α- and γ-subunits of 7S NGF to form a high molecular weight complex. In this behavior it resembles a modified form of mouse NGF which, like Naja naja NGF, lacks COOH-terminal arginine residues.",
author = "Server, {Alfred C.} and Karl Herrup and Shooter, {Eric M.} and Hogue-Angeletti, {Ruth A.} and Frazier, {William A.} and Bradshaw, {Ralph A.}",
year = "1976",
language = "English (US)",
volume = "15",
pages = "35--39",
journal = "Biochemistry",
issn = "0006-2960",
publisher = "American Chemical Society",
number = "1",

}

TY - JOUR

T1 - Comparison of the nerve growth factor proteins from cobra venom (Naja naja) and mouse submaxillary gland

AU - Server, Alfred C.

AU - Herrup, Karl

AU - Shooter, Eric M.

AU - Hogue-Angeletti, Ruth A.

AU - Frazier, William A.

AU - Bradshaw, Ralph A.

PY - 1976

Y1 - 1976

N2 - The nerve growth factors (NGF's) isolated from cobra venom (Naja naja) and mouse submaxillary gland are closely related proteins. They are structurally similar in that about 60% of their amino acid residues are identical (Hogue-Angeletti, R. A., Frazier, W. A., Jacobs, J. W., Niall, H. D., and Bradshaw, R. A. (1976), Biochemistry, preceding paper in this issue). They are functionally similar in that they both elicit maximum neurite outgrowth from chick embryonic dorsal root ganglia at the same protein concentration. However, the extent of the response is not as great with Naja naja NGF. The cobra NGF has an affinity close to that of mouse NGF for a major proportion of the specific NGF receptors on cells from dissociated embryonic dorsal root ganglia. Despite these similarities there are differences which can be detected between the two proteins. High concentrations of Naja naja NGF will not displace approximately 20% of the binding of mouse NGF to specific NGF receptors. Moreover, Naja naja NGF shows limited cross-reactivity with antiserum to mouse NGF in a competition radioimmunoassay, consistent with the extent of its amino acid sequence homology with mouse NGF. Naja naja NGF does not interact with the α- and γ-subunits of 7S NGF to form a high molecular weight complex. In this behavior it resembles a modified form of mouse NGF which, like Naja naja NGF, lacks COOH-terminal arginine residues.

AB - The nerve growth factors (NGF's) isolated from cobra venom (Naja naja) and mouse submaxillary gland are closely related proteins. They are structurally similar in that about 60% of their amino acid residues are identical (Hogue-Angeletti, R. A., Frazier, W. A., Jacobs, J. W., Niall, H. D., and Bradshaw, R. A. (1976), Biochemistry, preceding paper in this issue). They are functionally similar in that they both elicit maximum neurite outgrowth from chick embryonic dorsal root ganglia at the same protein concentration. However, the extent of the response is not as great with Naja naja NGF. The cobra NGF has an affinity close to that of mouse NGF for a major proportion of the specific NGF receptors on cells from dissociated embryonic dorsal root ganglia. Despite these similarities there are differences which can be detected between the two proteins. High concentrations of Naja naja NGF will not displace approximately 20% of the binding of mouse NGF to specific NGF receptors. Moreover, Naja naja NGF shows limited cross-reactivity with antiserum to mouse NGF in a competition radioimmunoassay, consistent with the extent of its amino acid sequence homology with mouse NGF. Naja naja NGF does not interact with the α- and γ-subunits of 7S NGF to form a high molecular weight complex. In this behavior it resembles a modified form of mouse NGF which, like Naja naja NGF, lacks COOH-terminal arginine residues.

UR - http://www.scopus.com/inward/record.url?scp=0017294091&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0017294091&partnerID=8YFLogxK

M3 - Article

VL - 15

SP - 35

EP - 39

JO - Biochemistry

JF - Biochemistry

SN - 0006-2960

IS - 1

ER -