Structure of the androgen dependent SVS VI protein as derived from cDNA

A. L. Schifman; P. E. Mansson; D. B. Carter; K. Yamada; M. M. Harris; S. E. Harris

doi:10.1016/0303-7207(88)90195-5

Structure of the androgen dependent SVS VI protein as derived from cDNA

A. L. Schifman, P. E. Mansson, D. B. Carter, K. Yamada, M. M. Harris, S. E. Harris

Producción científica: Article › revisión exhaustiva

9 Citas (Scopus)

Resumen

The 11S poly(A ⁺)RNA from rat seminal vesicle was cloned. By hybrid selection of clones reacting to the low molecular weight region of the US peak, a clone containing a new seminal vesicle cDNA sequence called SVS VI was isolated. The DNA sequence of two overlapping cDNAs (pSV24 and pSV33) is presented. The sequence of SVS VI was compared to the previously isolated SVS IV and SVS V cDNAS. Dot hybridization showed that SVS VI is androgen responsive after giving testosterone to castrated rats. The hydrophilicity was analyzed using standard Bionet procedures. All three proteins are extremely variable, rich in α-helix and very water soluble. The computer predicted hydrophilicity is compared for SVS VI, V and IV. A small region in the 3'-non-coding area of SVS VI has high similarity to a region in SVS IV mRNA.

Idioma original	English (US)
Páginas (desde-hasta)	57-65
Número de páginas	9
Publicación	Molecular and Cellular Endocrinology
Volumen	59
N.º	1-2
DOI	https://doi.org/10.1016/0303-7207(88)90195-5
Estado	Published - sept 1988
Publicado de forma externa	Sí

ASJC Scopus subject areas

Biochemistry
Molecular Biology
Endocrinology

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@article{28e2d4c885c84e3aa6037568883e4da9,

title = "Structure of the androgen dependent SVS VI protein as derived from cDNA",

abstract = "The 11S poly(A +)RNA from rat seminal vesicle was cloned. By hybrid selection of clones reacting to the low molecular weight region of the US peak, a clone containing a new seminal vesicle cDNA sequence called SVS VI was isolated. The DNA sequence of two overlapping cDNAs (pSV24 and pSV33) is presented. The sequence of SVS VI was compared to the previously isolated SVS IV and SVS V cDNAS. Dot hybridization showed that SVS VI is androgen responsive after giving testosterone to castrated rats. The hydrophilicity was analyzed using standard Bionet procedures. All three proteins are extremely variable, rich in α-helix and very water soluble. The computer predicted hydrophilicity is compared for SVS VI, V and IV. A small region in the 3'-non-coding area of SVS VI has high similarity to a region in SVS IV mRNA.",

keywords = "(Rat), Hormone regulation, SVS VI, androgen dependent, Seminal vesicle, mRNA accumulation, comparative",

author = "Schifman, {A. L.} and Mansson, {P. E.} and Carter, {D. B.} and K. Yamada and Harris, {M. M.} and Harris, {S. E.}",

year = "1988",

month = sep,

doi = "10.1016/0303-7207(88)90195-5",

language = "English (US)",

volume = "59",

pages = "57--65",

journal = "Molecular and Cellular Endocrinology",

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TY - JOUR

T1 - Structure of the androgen dependent SVS VI protein as derived from cDNA

AU - Schifman, A. L.

AU - Mansson, P. E.

AU - Carter, D. B.

AU - Yamada, K.

AU - Harris, M. M.

AU - Harris, S. E.

PY - 1988/9

Y1 - 1988/9

N2 - The 11S poly(A +)RNA from rat seminal vesicle was cloned. By hybrid selection of clones reacting to the low molecular weight region of the US peak, a clone containing a new seminal vesicle cDNA sequence called SVS VI was isolated. The DNA sequence of two overlapping cDNAs (pSV24 and pSV33) is presented. The sequence of SVS VI was compared to the previously isolated SVS IV and SVS V cDNAS. Dot hybridization showed that SVS VI is androgen responsive after giving testosterone to castrated rats. The hydrophilicity was analyzed using standard Bionet procedures. All three proteins are extremely variable, rich in α-helix and very water soluble. The computer predicted hydrophilicity is compared for SVS VI, V and IV. A small region in the 3'-non-coding area of SVS VI has high similarity to a region in SVS IV mRNA.

AB - The 11S poly(A +)RNA from rat seminal vesicle was cloned. By hybrid selection of clones reacting to the low molecular weight region of the US peak, a clone containing a new seminal vesicle cDNA sequence called SVS VI was isolated. The DNA sequence of two overlapping cDNAs (pSV24 and pSV33) is presented. The sequence of SVS VI was compared to the previously isolated SVS IV and SVS V cDNAS. Dot hybridization showed that SVS VI is androgen responsive after giving testosterone to castrated rats. The hydrophilicity was analyzed using standard Bionet procedures. All three proteins are extremely variable, rich in α-helix and very water soluble. The computer predicted hydrophilicity is compared for SVS VI, V and IV. A small region in the 3'-non-coding area of SVS VI has high similarity to a region in SVS IV mRNA.

KW - (Rat)

KW - Hormone regulation

KW - SVS VI, androgen dependent

KW - Seminal vesicle

KW - mRNA accumulation, comparative

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UR - http://www.scopus.com/inward/citedby.url?scp=0023765125&partnerID=8YFLogxK

U2 - 10.1016/0303-7207(88)90195-5

DO - 10.1016/0303-7207(88)90195-5

M3 - Article

C2 - 2848738

AN - SCOPUS:0023765125

SN - 0303-7207

VL - 59

SP - 57

EP - 65

JO - Molecular and Cellular Endocrinology

JF - Molecular and Cellular Endocrinology

IS - 1-2

ER -

Structure of the androgen dependent SVS VI protein as derived from cDNA

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